OSGL1_XENTR
ID OSGL1_XENTR Reviewed; 405 AA.
AC Q0P4K0;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 2.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=tRNA N6-adenosine threonylcarbamoyltransferase, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03179};
DE EC=2.3.1.234 {ECO:0000255|HAMAP-Rule:MF_03179};
DE AltName: Full=N6-L-threonylcarbamoyladenine synthase {ECO:0000255|HAMAP-Rule:MF_03179};
DE Short=t(6)A synthase {ECO:0000255|HAMAP-Rule:MF_03179};
DE AltName: Full=O-sialoglycoprotein endopeptidase-like protein 1 {ECO:0000255|HAMAP-Rule:MF_03179};
DE AltName: Full=t(6)A37 threonylcarbamoyladenosine biosynthesis protein osgepl1 {ECO:0000255|HAMAP-Rule:MF_03179};
DE AltName: Full=tRNA threonylcarbamoyladenosine biosynthesis protein osgepl1 {ECO:0000255|HAMAP-Rule:MF_03179};
DE Flags: Precursor;
GN Name=osgepl1 {ECO:0000255|HAMAP-Rule:MF_03179};
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=N6; TISSUE=Ovary;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Required for the formation of a threonylcarbamoyl group on
CC adenosine at position 37 (t(6)A37) in mitochondrial tRNAs that read
CC codons beginning with adenine. Probably involved in the transfer of the
CC threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6
CC group of A37. Involved in mitochondrial genome maintenance.
CC {ECO:0000255|HAMAP-Rule:MF_03179}.
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_03179};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03179};
CC Note=Binds 1 divalent metal cation per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_03179};
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_03179}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03179}.
CC -!- SIMILARITY: Belongs to the KAE1 / TsaD family. {ECO:0000255|HAMAP-
CC Rule:MF_03179}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI22039.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BC122038; AAI22039.1; ALT_INIT; mRNA.
DR RefSeq; NP_001153459.1; NM_001159987.1.
DR RefSeq; XP_012825973.1; XM_012970519.2.
DR RefSeq; XP_012825974.1; XM_012970520.2.
DR AlphaFoldDB; Q0P4K0; -.
DR SMR; Q0P4K0; -.
DR STRING; 8364.ENSXETP00000062148; -.
DR PaxDb; Q0P4K0; -.
DR GeneID; 779499; -.
DR KEGG; xtr:779499; -.
DR CTD; 64172; -.
DR Xenbase; XB-GENE-948324; osgepl1.
DR eggNOG; KOG2707; Eukaryota.
DR HOGENOM; CLU_023208_1_2_1; -.
DR InParanoid; Q0P4K0; -.
DR OrthoDB; 656684at2759; -.
DR TreeFam; TF314600; -.
DR Proteomes; UP000008143; Chromosome 9.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000009883; Expressed in egg cell and 13 other tissues.
DR ExpressionAtlas; Q0P4K0; baseline.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061711; F:N(6)-L-threonylcarbamoyladenine synthase activity; ISS:UniProtKB.
DR GO; GO:0002949; P:tRNA threonylcarbamoyladenosine modification; ISS:UniProtKB.
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; 1.
DR TIGRFAMs; TIGR00329; gcp_kae1; 1.
PE 2: Evidence at transcript level;
KW Acyltransferase; Metal-binding; Mitochondrion; Reference proteome;
KW Transferase; Transit peptide; tRNA processing.
FT TRANSIT 1..19
FT /note="Mitochondrion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03179"
FT CHAIN 20..405
FT /note="tRNA N6-adenosine threonylcarbamoyltransferase,
FT mitochondrial"
FT /id="PRO_0000307782"
FT BINDING 138
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03179"
FT BINDING 142
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03179"
FT BINDING 160..164
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03179"
FT BINDING 193
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03179"
FT BINDING 213
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03179"
FT BINDING 217
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03179"
FT BINDING 320..321
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03179"
FT BINDING 348
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03179"
FT BINDING 349
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03179"
SQ SEQUENCE 405 AA; 43813 MW; 46D27D881916D7C7 CRC64;
MAKYISNLSR IAVVRGRVSV STLVKYPRIV LGIETSCDDT GAAVVDENGT ILGEALHCQK
DIHLKTGGII PTVAQHLHRD NITKVVNKAI HASGISPYEL SAIATTVKPG LGLCLGVGLS
YSLDLVNKYH KPFIPIHHME AHALTVRLLH PVEFPFLVLL ISGGHCILAI VSGVSEFVML
GHSLDEAPGD TLDKVARRLS LINHPQCSGM SGGEAIEHLA LHGNRKICKL KIPMSHHRDC
NFSFAGLRNQ VNKVIEQKEA EKGISKGQLL PCVADIAAAV QHTVALHLAQ RTQRAIYYCK
REGLIPTERA CLVVSGGVAS NRYIRKALQT VTHESDMTLL CPPPRLCTDN GVMIAWNGIE
KLQSGVGVLH NADGACYESR ASLGRDISEL VRKAAIKVQP IKILS
