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TSAD_BRUA4
ID   TSAD_BRUA4              Reviewed;         359 AA.
AC   A6WXJ1;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 89.
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=Oant_0974;
OS   Brucella anthropi (strain ATCC 49188 / DSM 6882 / CCUG 24695 / JCM 21032 /
OS   LMG 3331 / NBRC 15819 / NCTC 12168 / Alc 37) (Ochrobactrum anthropi).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=439375;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49188 / DSM 6882 / CCUG 24695 / JCM 21032 / LMG 3331 / NBRC
RC   15819 / NCTC 12168 / Alc 37;
RX   PubMed=21685287; DOI=10.1128/jb.05335-11;
RA   Chain P.S., Lang D.M., Comerci D.J., Malfatti S.A., Vergez L.M., Shin M.,
RA   Ugalde R.A., Garcia E., Tolmasky M.E.;
RT   "Genome of Ochrobactrum anthropi ATCC 49188 T, a versatile opportunistic
RT   pathogen and symbiont of several eukaryotic hosts.";
RL   J. Bacteriol. 193:4274-4275(2011).
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;
CC         Evidence={ECO:0000255|HAMAP-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; CP000758; ABS13695.1; -; Genomic_DNA.
DR   RefSeq; WP_012091158.1; NC_009667.1.
DR   AlphaFoldDB; A6WXJ1; -.
DR   SMR; A6WXJ1; -.
DR   STRING; 439375.Oant_0974; -.
DR   EnsemblBacteria; ABS13695; ABS13695; Oant_0974.
DR   KEGG; oan:Oant_0974; -.
DR   PATRIC; fig|439375.7.peg.1020; -.
DR   eggNOG; COG0533; Bacteria.
DR   HOGENOM; CLU_023208_0_2_5; -.
DR   OMA; HLEGHIY; -.
DR   OrthoDB; 1257362at2; -.
DR   PhylomeDB; A6WXJ1; -.
DR   Proteomes; UP000002301; Chromosome 1.
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   HAMAP; MF_01445; TsaD; 1.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR000905; Gcp-like_dom.
DR   InterPro; IPR017861; KAE1/TsaD.
DR   InterPro; IPR022450; TsaD.
DR   PANTHER; PTHR11735; PTHR11735; 1.
DR   PANTHER; PTHR11735:SF6; PTHR11735:SF6; 1.
DR   Pfam; PF00814; TsaD; 1.
DR   PRINTS; PR00789; OSIALOPTASE.
DR   SUPFAM; SSF53067; SSF53067; 2.
DR   TIGRFAMs; TIGR00329; gcp_kae1; 1.
DR   TIGRFAMs; TIGR03723; T6A_TsaD_YgjD; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Cytoplasm; Iron; Metal-binding; Reference proteome;
KW   Transferase; tRNA processing.
FT   CHAIN           1..359
FT                   /note="tRNA N6-adenosine threonylcarbamoyltransferase"
FT                   /id="PRO_1000024439"
FT   REGION          328..359
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         115
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01445"
FT   BINDING         119
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01445"
FT   BINDING         137..141
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01445"
FT   BINDING         170
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01445"
FT   BINDING         183
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01445"
FT   BINDING         283
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01445"
FT   BINDING         311
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01445"
SQ   SEQUENCE   359 AA;  37852 MW;  8856BBED812A6C1D CRC64;
     MRILGIETSC DETAAAIVER DGQGEGRILS NVVLSQIAEH EPYGGVVPEI AARAHVEALD
     RLVARALEDA DMKLADVDAV AATAGPGLIG GLIVGLMTAK ALAMAAQKPF YAVNHLEGHA
     LTARLTDGLP FPYLLLLVSG GHTQMVLIRG IGDYERLGTT IDDALGEAFD KTAKLLGLPY
     PGGPAVERMA LQGNPKRFAL PRPLKGEARL DFSFSGLKTA VRQTATELVP LSDQDVADIC
     ASFQAAVADT LSDRVGRSLE RFRNEFPDCE TPALVVAGGV AANKTLRAAL ETLCARHGFS
     FIAPPLDLCT DNAAMIAWAG AERAATEAPD SLDLAPRSRW PLDEKSAPLI GTGRRGAKA
 
 
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