TYW5_DANRE
ID TYW5_DANRE Reviewed; 326 AA.
AC Q08BV2;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=tRNA wybutosine-synthesizing protein 5 {ECO:0000305};
DE EC=1.14.11.42 {ECO:0000250|UniProtKB:A2RUC4};
DE AltName: Full=tRNA(Phe) (7-(3-amino-3-carboxypropyl)wyosine(37)-C(2))-hydroxylase;
GN Name=tyw5; ORFNames=zgc:154110;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: tRNA hydroxylase that acts as a component of the wybutosine
CC biosynthesis pathway. Wybutosine is a hyper modified guanosine with a
CC tricyclic base found at the 3'-position adjacent to the anticodon of
CC eukaryotic phenylalanine tRNA. Catalyzes the hydroxylation of 7-(a-
CC amino-a-carboxypropyl)wyosine (yW-72) into undermodified
CC hydroxywybutosine (OHyW*). OHyW* being further transformed into
CC hydroxywybutosine (OHyW) by LCMT2/TYW4. OHyW is a derivative of
CC wybutosine found in higher eukaryotes. {ECO:0000250|UniProtKB:A2RUC4}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + 7-[(3S)-3-amino-3-carboxypropyl]wyosine(37)
CC in tRNA(Phe) + O2 = 7-(2-hydroxy-3-amino-3-carboxypropyl)wyosine(37)
CC in tRNA(Phe) + CO2 + succinate; Xref=Rhea:RHEA:37899, Rhea:RHEA-
CC COMP:10379, Rhea:RHEA-COMP:11848, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031,
CC ChEBI:CHEBI:73543, ChEBI:CHEBI:73603; EC=1.14.11.42;
CC Evidence={ECO:0000250|UniProtKB:A2RUC4};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37900;
CC Evidence={ECO:0000250|UniProtKB:A2RUC4};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000250|UniProtKB:A2RUC4};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000250|UniProtKB:A2RUC4};
CC -!- PATHWAY: tRNA modification; wybutosine-tRNA(Phe) biosynthesis.
CC {ECO:0000250|UniProtKB:A2RUC4}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:A2RUC4}.
CC -!- SIMILARITY: Belongs to the TYW5 family. {ECO:0000305}.
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DR EMBL; BC124543; AAI24544.1; -; mRNA.
DR RefSeq; NP_001071011.1; NM_001077543.1.
DR AlphaFoldDB; Q08BV2; -.
DR SMR; Q08BV2; -.
DR STRING; 7955.ENSDARP00000092344; -.
DR PaxDb; Q08BV2; -.
DR GeneID; 557725; -.
DR KEGG; dre:557725; -.
DR CTD; 129450; -.
DR ZFIN; ZDB-GENE-060929-894; tyw5.
DR eggNOG; KOG2132; Eukaryota.
DR InParanoid; Q08BV2; -.
DR OrthoDB; 1385616at2759; -.
DR PhylomeDB; Q08BV2; -.
DR UniPathway; UPA00375; -.
DR PRO; PR:Q08BV2; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0016706; F:2-oxoglutarate-dependent dioxygenase activity; IBA:GO_Central.
DR GO; GO:0005506; F:iron ion binding; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0000049; F:tRNA binding; ISS:UniProtKB.
DR GO; GO:0102524; F:tRNAPhe (7-(3-amino-3-carboxypropyl)wyosine37-C2)-hydroxylase activity; ISS:UniProtKB.
DR GO; GO:0031591; P:wybutosine biosynthetic process; ISS:UniProtKB.
DR InterPro; IPR041667; Cupin_8.
DR InterPro; IPR003347; JmjC_dom.
DR InterPro; IPR029612; TYW5.
DR PANTHER; PTHR12461:SF50; PTHR12461:SF50; 1.
DR Pfam; PF13621; Cupin_8; 1.
DR SMART; SM00558; JmjC; 1.
DR PROSITE; PS51184; JMJC; 1.
PE 2: Evidence at transcript level;
KW Dioxygenase; Iron; Metal-binding; Oxidoreductase; Reference proteome;
KW tRNA processing.
FT CHAIN 1..326
FT /note="tRNA wybutosine-synthesizing protein 5"
FT /id="PRO_0000309276"
FT DOMAIN 106..268
FT /note="JmjC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 107
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250"
FT BINDING 161
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 163
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 167
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250"
FT BINDING 176
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250"
FT BINDING 236
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
SQ SEQUENCE 326 AA; 38059 MW; 079414C219BEB08C CRC64;
MDCQEKLEVP VYTDVDKETF LRDIYPQRRP AVLKRVPIGP CVRTWTVCFL AEKGGDREVK
VHVSPEPRMD FLHKNFVYRT LPFDEFIKRA AEAKHPEFFI SEDESYYLRS LGEDARKEPA
DLRKQFPELA EDFHVPQFFE PEQFFSSVFR ISSPGLQLWT HYDVMDNLLA QVTGKKRVVL
YSPEDALHLY LTGDKSEVLD IDSPDLQLYP EFVKARRYEC ILEPGDLLFI PALWFHNTLA
LQFGVGVNVF WRHLPSESYD KKDPYGNKDP VAATRALQSL ERTLGILDEL PPDYRDFYAR
RMVLRIQSRA YIRKPINAAQ ENSDTT
