ID   TSAD_ACIAD              Reviewed;         340 AA.
AC   Q6FCK9;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   07-JAN-2015, entry version 73.
DE   RecName: Full=tRNA N6-adenosine threonylcarbamoyltransferase {ECO:0000255|HAMAP-Rule:MF_01445};
DE            EC=2.6.99.4 {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=ACIAD1332;
OS   Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Moraxellaceae; Acinetobacter.
OX   NCBI_TaxID=62977;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33305 / BD413 / ADP1;
RX   PubMed=15514110; DOI=10.1093/nar/gkh910;
RA   Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S.,
RA   Labarre L., Cruveiller S., Robert C., Duprat S., Wincker P.,
RA   Ornston L.N., Weissenbach J., Marliere P., Cohen G.N., Medigue C.;
RT   "Unique features revealed by the genome sequence of Acinetobacter sp.
RT   ADP1, a versatile and naturally transformation competent bacterium.";
RL   Nucleic Acids Res. 32:5766-5779(2004).
CC   -!- FUNCTION: Required for the formation of a threonylcarbamoyl group
CC       on adenosine at position 37 (t(6)A37) in tRNAs that read codons
CC       beginning with adenine. Is involved in the transfer of the
CC       threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the
CC       N6 group of A37, together with TsaE and TsaB. TsaD likely plays a
CC       direct catalytic role in this reaction. {ECO:0000255|HAMAP-
CC       Rule:MF_01445}.
CC   -!- CATALYTIC ACTIVITY: L-threonylcarbamoyladenylate + adenine(37) in
CC       tRNA = AMP + N(6)-L-threonylcarbamoyladenine(37) in tRNA.
CC       {ECO:0000255|HAMAP-Rule:MF_01445}.
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01445};
CC       Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000255|HAMAP-
CC       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; CR543861; CAG68201.1; -; Genomic_DNA.
DR   RefSeq; YP_046023.1; NC_005966.1.
DR   ProteinModelPortal; Q6FCK9; -.
DR   STRING; 62977.ACIAD1332; -.
DR   EnsemblBacteria; CAG68201; CAG68201; ACIAD1332.
DR   GeneID; 2879625; -.
DR   KEGG; aci:ACIAD1332; -.
DR   PATRIC; 20740477; VBIAciSp98416_1197.
DR   eggNOG; COG0533; -.
DR   HOGENOM; HOG000109568; -.
DR   KO; K01409; -.
DR   OMA; EVNHMQA; -.
DR   OrthoDB; EOG6K402S; -.
DR   BioCyc; ASP62977:GJVV-1258-MONOMER; -.
DR   Proteomes; UP000000430; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0016747; F:transferase activity, transferring acyl groups other than amino-acyl groups; IEA:UniProtKB-HAMAP.
DR   GO; GO:0070526; P:threonylcarbamoyladenosine biosynthetic process; IEA:UniProtKB-HAMAP.
DR   HAMAP; MF_01445; TsaD; 1.
DR   InterPro; IPR000905; Gcp-like_dom.
DR   InterPro; IPR017861; KAE1/YgjD.
DR   InterPro; IPR017860; Peptidase_M22_CS.
DR   InterPro; IPR022450; TsaD.
DR   Pfam; PF00814; Peptidase_M22; 1.
DR   PRINTS; PR00789; OSIALOPTASE.
DR   TIGRFAMs; TIGR00329; gcp_kae1; 1.
DR   TIGRFAMs; TIGR03723; T6A_YgjD; 1.
DR   PROSITE; PS01016; GLYCOPROTEASE; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Complete proteome; Cytoplasm; Iron; Metal-binding;
KW   Reference proteome; Transferase; tRNA processing.
FT   CHAIN         1    340       tRNA N6-adenosine
FT                                threonylcarbamoyltransferase.
FT                                /FTId=PRO_0000303245.
FT   REGION      134    138       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_01445}.
FT   METAL       111    111       Iron. {ECO:0000255|HAMAP-Rule:MF_01445}.
FT   METAL       115    115       Iron. {ECO:0000255|HAMAP-Rule:MF_01445}.
FT   METAL       298    298       Iron. {ECO:0000255|HAMAP-Rule:MF_01445}.
FT   BINDING     167    167       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01445}.
FT   BINDING     180    180       Substrate; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01445}.
FT   BINDING     270    270       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01445}.
SQ   SEQUENCE   340 AA;  36723 MW;  E0384A9EAE3B2460 CRC64;
     MIVLGLETSC DETGLALYDS EKGLLGQVLY SQIKLHAEYG GVVPELASRD HVRKMIPLLD
     QLLNDSQVKK SQIDAVAYTR GPGLMGALMT GALFGRTLAF ALNKPAIGVH HMEGHMLAPL
     LSATPPEFPF VALLVSGGHT QLMAAYGIGQ YELLGESIDD AAGEAFDKVA KMMGLPYPGG
     PNIAKLALQG NPETFEFPRP MLHQGLDFSF SGLKTSVSVQ LKKLGEENRD ADIAASFQEA
     IVDTLVKKSV KALKQTGLKR LVIAGGVSAN QRLRERLEHS LSKIKSQVYY AEPALCTDNG
     AMIAFAGYQR LKAGQCDDLV VTTTPRWPMT ELSRPAEIIE
//