TYW5_CHICK
ID TYW5_CHICK Reviewed; 318 AA.
AC E1C7T6;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2010, sequence version 1.
DT 03-AUG-2022, entry version 57.
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;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15592404; DOI=10.1038/nature03154;
RA Hillier L.W., Miller W., Birney E., Warren W., Hardison R.C., Ponting C.P.,
RA Bork P., Burt D.W., Groenen M.A.M., Delany M.E., Dodgson J.B.,
RA Chinwalla A.T., Cliften P.F., Clifton S.W., Delehaunty K.D., Fronick C.,
RA Fulton R.S., Graves T.A., Kremitzki C., Layman D., Magrini V.,
RA McPherson J.D., Miner T.L., Minx P., Nash W.E., Nhan M.N., Nelson J.O.,
RA Oddy L.G., Pohl C.S., Randall-Maher J., Smith S.M., Wallis J.W.,
RA Yang S.-P., Romanov M.N., Rondelli C.M., Paton B., Smith J., Morrice D.,
RA Daniels L., Tempest H.G., Robertson L., Masabanda J.S., Griffin D.K.,
RA Vignal A., Fillon V., Jacobbson L., Kerje S., Andersson L.,
RA Crooijmans R.P., Aerts J., van der Poel J.J., Ellegren H., Caldwell R.B.,
RA Hubbard S.J., Grafham D.V., Kierzek A.M., McLaren S.R., Overton I.M.,
RA Arakawa H., Beattie K.J., Bezzubov Y., Boardman P.E., Bonfield J.K.,
RA Croning M.D.R., Davies R.M., Francis M.D., Humphray S.J., Scott C.E.,
RA Taylor R.G., Tickle C., Brown W.R.A., Rogers J., Buerstedde J.-M.,
RA Wilson S.A., Stubbs L., Ovcharenko I., Gordon L., Lucas S., Miller M.M.,
RA Inoko H., Shiina T., Kaufman J., Salomonsen J., Skjoedt K., Wong G.K.-S.,
RA Wang J., Liu B., Wang J., Yu J., Yang H., Nefedov M., Koriabine M.,
RA Dejong P.J., Goodstadt L., Webber C., Dickens N.J., Letunic I., Suyama M.,
RA Torrents D., von Mering C., Zdobnov E.M., Makova K., Nekrutenko A.,
RA Elnitski L., Eswara P., King D.C., Yang S.-P., Tyekucheva S.,
RA Radakrishnan A., Harris R.S., Chiaromonte F., Taylor J., He J.,
RA Rijnkels M., Griffiths-Jones S., Ureta-Vidal A., Hoffman M.M., Severin J.,
RA Searle S.M.J., Law A.S., Speed D., Waddington D., Cheng Z., Tuzun E.,
RA Eichler E., Bao Z., Flicek P., Shteynberg D.D., Brent M.R., Bye J.M.,
RA Huckle E.J., Chatterji S., Dewey C., Pachter L., Kouranov A.,
RA Mourelatos Z., Hatzigeorgiou A.G., Paterson A.H., Ivarie R., Brandstrom M.,
RA Axelsson E., Backstrom N., Berlin S., Webster M.T., Pourquie O.,
RA Reymond A., Ucla C., Antonarakis S.E., Long M., Emerson J.J., Betran E.,
RA Dupanloup I., Kaessmann H., Hinrichs A.S., Bejerano G., Furey T.S.,
RA Harte R.A., Raney B., Siepel A., Kent W.J., Haussler D., Eyras E.,
RA Castelo R., Abril J.F., Castellano S., Camara F., Parra G., Guigo R.,
RA Bourque G., Tesler G., Pevzner P.A., Smit A., Fulton L.A., Mardis E.R.,
RA Wilson R.K.;
RT "Sequence and comparative analysis of the chicken genome provide unique
RT perspectives on vertebrate evolution.";
RL Nature 432:695-716(2004).
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; AADN02019856; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; E1C7T6; -.
DR SMR; E1C7T6; -.
DR STRING; 9031.ENSGALP00000013215; -.
DR PaxDb; E1C7T6; -.
DR Ensembl; ENSGALT00000013230; ENSGALP00000013215; ENSGALG00000008145.
DR VEuPathDB; HostDB:geneid_424065; -.
DR eggNOG; KOG2132; Eukaryota.
DR GeneTree; ENSGT00940000158493; -.
DR InParanoid; E1C7T6; -.
DR OMA; PLYDDRP; -.
DR OrthoDB; 1385616at2759; -.
DR PhylomeDB; E1C7T6; -.
DR TreeFam; TF332364; -.
DR UniPathway; UPA00375; -.
DR PRO; PR:E1C7T6; -.
DR Proteomes; UP000000539; Chromosome 7.
DR Bgee; ENSGALG00000008145; Expressed in granulocyte and 13 other tissues.
DR ExpressionAtlas; E1C7T6; baseline and differential.
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 3: Inferred from homology;
KW Dioxygenase; Iron; Metal-binding; Oxidoreductase; Reference proteome;
KW tRNA processing.
FT CHAIN 1..318
FT /note="tRNA wybutosine-synthesizing protein 5"
FT /id="PRO_0000404592"
FT DOMAIN 126..270
FT /note="JmjC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 109
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250"
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 165
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 169
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250"
FT BINDING 178
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250"
FT BINDING 238
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
SQ SEQUENCE 318 AA; 37244 MW; F6A85D8306DFF7B3 CRC64;
MEQREQPAVQ VPSLDGVTRE RFLRDVYPRR EPVVLKGMEL GPCTTKWTVD YLSQAAGSKE
VKIHVSAVPQ MDFLSKNFVY RTLPFDVFVR RAAEVKHKDY FLSEDEKYYL RSVGEDVRKD
IADIRKQFPV LAEDVQIPEY FEKEQFFSSV FRISSAGLQL WTHYDVMDNF LIQVTGRKRV
VLYSPRDVPY LYLSGTKSEV LDVDNPDFEK YPLFAKAKRY QCYLEAGDVL FIPAMWFHNV
ISEEFGVALN VFWKHLPAEC YDKSDTYGNK DPTAASRAIQ ILDRALKTLE ELPEEYRDFY
ARRMVLRIQE KAYRNDNG
