TSAD_METPP
ID TSAD_METPP Reviewed; 348 AA.
AC A2SFL8;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 2.
DT 03-AUG-2022, entry version 84.
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=Mpe_A1395;
OS Methylibium petroleiphilum (strain ATCC BAA-1232 / LMG 22953 / PM1).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; Methylibium.
OX NCBI_TaxID=420662;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1232 / LMG 22953 / PM1;
RX PubMed=17158667; DOI=10.1128/jb.01259-06;
RA Kane S.R., Chakicherla A.Y., Chain P.S.G., Schmidt R., Shin M.W.,
RA Legler T.C., Scow K.M., Larimer F.W., Lucas S.M., Richardson P.M.,
RA Hristova K.R.;
RT "Whole-genome analysis of the methyl tert-butyl ether-degrading beta-
RT proteobacterium Methylibium petroleiphilum PM1.";
RL J. Bacteriol. 189:1931-1945(2007).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABM94357.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000555; ABM94357.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_036230548.1; NC_008825.1.
DR AlphaFoldDB; A2SFL8; -.
DR SMR; A2SFL8; -.
DR STRING; 420662.Mpe_A1395; -.
DR EnsemblBacteria; ABM94357; ABM94357; Mpe_A1395.
DR KEGG; mpt:Mpe_A1395; -.
DR eggNOG; COG0533; Bacteria.
DR HOGENOM; CLU_023208_0_2_4; -.
DR OrthoDB; 1257362at2; -.
DR Proteomes; UP000000366; 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 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 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.
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..348
FT /note="tRNA N6-adenosine threonylcarbamoyltransferase"
FT /id="PRO_0000303423"
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 138..142
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01445"
FT BINDING 171
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01445"
FT BINDING 184
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01445"
FT BINDING 278
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01445"
FT BINDING 306
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01445"
SQ SEQUENCE 348 AA; 36450 MW; 7B2897001838E5D1 CRC64;
MLILGFESSC DETGVALVAA DHGERPRLLA HALHSQVAMH EAYGGVVPEL ASRDHIRRAL
PLTRQVLAEA GRALADVDVV AYTRGPGLAG ALLVGSAVAC ALAAALDRPV LGIHHLEGHL
LSPFLSVDPP QFPFVALLVS GGHTQLMRVD GVGDYALLGE TIDDAAGEAF DKSAKLLGLG
YPGGPALARL AEFGDPTAYA LPRPLLHRDT LDFSFAGLKT AVRTQVLKLG EGVCEQPRAD
LAAATQAAIV EVLVKKSLAA LRATRLQRLV VAGGVGANRS LRSQLDAACA KRGVRVHYPE
VSLCTDNGAM IALAAAMRLQ AGRATARRDH AFDVQPRWPL AALDVGVP
