ID   KAE1_SULIN              Reviewed;         331 AA.
AC   C3NGI3;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 1.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=tRNA N6-adenosine threonylcarbamoyltransferase {ECO:0000255|HAMAP-Rule:MF_01446};
DE            EC=2.3.1.234 {ECO:0000255|HAMAP-Rule:MF_01446};
DE   AltName: Full=N6-L-threonylcarbamoyladenine synthase {ECO:0000255|HAMAP-Rule:MF_01446};
DE            Short=t(6)A synthase {ECO:0000255|HAMAP-Rule:MF_01446};
DE   AltName: Full=t(6)A37 threonylcarbamoyladenosine biosynthesis protein Kae1 {ECO:0000255|HAMAP-Rule:MF_01446};
DE   AltName: Full=tRNA threonylcarbamoyladenosine biosynthesis protein Kae1 {ECO:0000255|HAMAP-Rule:MF_01446};
GN   Name=kae1 {ECO:0000255|HAMAP-Rule:MF_01446}; OrderedLocusNames=YN1551_1137;
OS   Sulfolobus islandicus (strain Y.N.15.51 / Yellowstone #2).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfolobus.
OX   NCBI_TaxID=419942;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y.N.15.51 / Yellowstone #2;
RX   PubMed=19435847; DOI=10.1073/pnas.0808945106;
RA   Reno M.L., Held N.L., Fields C.J., Burke P.V., Whitaker R.J.;
RT   "Biogeography of the Sulfolobus islandicus pan-genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:8605-8610(2009).
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 probably involved in the transfer of the
CC       threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6
CC       group of A37. {ECO:0000255|HAMAP-Rule:MF_01446}.
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_01446};
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01446};
CC       Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01446};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01446}.
CC   -!- SIMILARITY: Belongs to the KAE1 / TsaD family. {ECO:0000255|HAMAP-
CC       Rule:MF_01446}.
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DR   EMBL; CP001404; ACP48243.1; -; Genomic_DNA.
DR   RefSeq; WP_012717350.1; NC_012623.1.
DR   AlphaFoldDB; C3NGI3; -.
DR   SMR; C3NGI3; -.
DR   EnsemblBacteria; ACP48243; ACP48243; YN1551_1137.
DR   GeneID; 7809997; -.
DR   KEGG; sin:YN1551_1137; -.
DR   HOGENOM; CLU_023208_2_2_2; -.
DR   OMA; MRIMCEE; -.
DR   Proteomes; UP000006818; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0000408; C:EKC/KEOPS complex; IEA:InterPro.
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_01446; Kae1; 1.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR000905; Gcp-like_dom.
DR   InterPro; IPR017861; KAE1/TsaD.
DR   InterPro; IPR022449; Kae1_arc.
DR   InterPro; IPR034680; Kae1_archaea_euk.
DR   PANTHER; PTHR11735; PTHR11735; 1.
DR   PANTHER; PTHR11735:SF14; PTHR11735:SF14; 1.
DR   Pfam; PF00814; TsaD; 1.
DR   PRINTS; PR00789; OSIALOPTASE.
DR   SUPFAM; SSF53067; SSF53067; 1.
DR   TIGRFAMs; TIGR03722; arch_KAE1; 1.
DR   TIGRFAMs; TIGR00329; gcp_kae1; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Cytoplasm; Iron; Metal-binding; Transferase;
KW   tRNA processing.
FT   CHAIN           1..331
FT                   /note="tRNA N6-adenosine threonylcarbamoyltransferase"
FT                   /id="PRO_1000215317"
FT   BINDING         109
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01446"
FT   BINDING         113
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01446"
FT   BINDING         130..134
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01446"
FT   BINDING         130
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01446"
FT   BINDING         162
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01446"
FT   BINDING         183
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01446"
FT   BINDING         262
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01446"
FT   BINDING         290
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01446"
SQ   SEQUENCE   331 AA;  36204 MW;  DE1851F41FA28FA0 CRC64;
     MLVLGIESTA HTFGVGIAKD QPPYILANER DAFVPKEGGM KPGDLLKHHA EASGTILRRA
     LEKANISIND INYIAVALGP GIGPALRVGA TLARALSLKY NKKLVPVNHS IGHIEIGYLT
     TEAKDPLILY LSGGNTIITT FYKGRFRIFG ETLDIALGNM MDVFVREVNL APPYIINGKH
     AIDICSEKGS KLLKLPYVVK GQDMSFSGLL TAALRLVGKE KLEDICYSIR EIAFDMLLEA
     TERALALTSK KELMIVGGVA ASVSLRKKLE ELGKEWDVQI KIVPPEFAGD NGAMIAYAGM
     LAASKGVFID VDKSYIRPRW RVDEVDIPWR N