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KAE1_SACS2
ID   KAE1_SACS2              Reviewed;         331 AA.
AC   Q97ZY8; E0A3F4;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-DEC-2013, sequence version 2.
DT   03-AUG-2022, entry version 109.
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=SSO0434;
OS   Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS   (Sulfolobus solfataricus).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Saccharolobus.
OX   NCBI_TaxID=273057;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RA   Hecker A.;
RT   "An update of the SSO0434 gene sequence from the archaeon Sulfolobus
RT   solfataricus.";
RL   Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RA   Hecker A.;
RT   "An update of the SSO5844-SSO0434-SSO0433 genomic region of the archaea
RT   Sulfolobus solfataricus P2.";
RL   Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX   PubMed=11427726; DOI=10.1073/pnas.141222098;
RA   She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA   Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA   Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA   Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA   Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA   Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT   "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAK40758.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; HM366920; ADK39020.1; -; Genomic_DNA.
DR   EMBL; HM370296; ADK88910.1; -; Genomic_DNA.
DR   EMBL; AE006641; AAK40758.1; ALT_FRAME; Genomic_DNA.
DR   PIR; G90187; G90187.
DR   AlphaFoldDB; Q97ZY8; -.
DR   SMR; Q97ZY8; -.
DR   STRING; 273057.SSO0434; -.
DR   DNASU; 1455568; -.
DR   EnsemblBacteria; AAK40758; AAK40758; SSO0434.
DR   KEGG; sso:SSO0434; -.
DR   PATRIC; fig|273057.12.peg.426; -.
DR   eggNOG; arCOG01183; Archaea.
DR   HOGENOM; CLU_023208_2_2_2; -.
DR   InParanoid; Q97ZY8; -.
DR   Proteomes; UP000001974; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0000408; C:EKC/KEOPS complex; IBA:GO_Central.
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; Reference proteome;
KW   Transferase; tRNA processing.
FT   CHAIN           1..331
FT                   /note="tRNA N6-adenosine threonylcarbamoyltransferase"
FT                   /id="PRO_0000303645"
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;  36290 MW;  F89341F2AF0C6BD1 CRC64;
     MFVLGIESTA HTFGVGIVRD SPPYILANER DTFIPKEGGM KPGDLLKHHA EVSATILRRA
     LEKAKISIND INYIAVALGP GIGPALRVGA TLARAIALKY NKKLVPVNHG IGHIEIGYLT
     TEARDPLILY LSGGNTIITT FYKGRFRVFG ETLDIALGNM MDVFVREVSL APPYIINGIH
     VIDICAEKGN KLLKLPYVVK GQDMSFSGLL TAALRVVGKE KLEDICYSVR EIAFDMLLEA
     TERALALTSK KELMIVGGVA ASVSLRKKLE ELGKEWNVQI KIVPPEFAGD NGAMIAYAGM
     LAASKGVFID VDKSYIRPRW RVDEVDIPWR N
 
 
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