IYD_DANRE
ID IYD_DANRE Reviewed; 295 AA.
AC E7FDV5;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 08-MAR-2011, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Iodotyrosine deiodinase {ECO:0000303|PubMed:24153409};
DE EC=1.21.1.1 {ECO:0000269|PubMed:24153409};
DE AltName: Full=Halotyrosine dehalogenase {ECO:0000305|PubMed:24153409};
GN Name=iyd; Synonyms=si:ch211-286f9.2;
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 {ECO:0000312|Proteomes:UP000000437};
RN [1] {ECO:0000312|Proteomes:UP000000437}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND COFACTOR.
RX PubMed=24153409; DOI=10.1039/c3mb70398c;
RA Phatarphekar A., Buss J.M., Rokita S.E.;
RT "Iodotyrosine deiodinase: a unique flavoprotein present in organisms of
RT diverse phyla.";
RL Mol. Biosyst. 10:86-92(2014).
CC -!- FUNCTION: Catalyzes the dehalogenation of halotyrosines such as 3,5-
CC diiodo-L-tyrosine (PubMed:24153409). Likely to also catalyze the
CC dehalogenation of other halotyrosines such as 3-bromo-L-tyrosine, 3-
CC chloro-L-tyrosine and 3-iodo-L-tyrosine (By similarity).
CC {ECO:0000250|UniProtKB:Q6PHW0, ECO:0000269|PubMed:24153409}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 iodide + L-tyrosine + 2 NADP(+) = 3,5-diiodo-L-tyrosine +
CC H(+) + 2 NADPH; Xref=Rhea:RHEA:32479, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16382, ChEBI:CHEBI:57506, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58315, ChEBI:CHEBI:58349; EC=1.21.1.1;
CC Evidence={ECO:0000269|PubMed:24153409};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:32481;
CC Evidence={ECO:0000269|PubMed:24153409};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=iodide + L-tyrosine + NADP(+) = 3-iodo-L-tyrosine + NADPH;
CC Xref=Rhea:RHEA:27453, ChEBI:CHEBI:16382, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58315, ChEBI:CHEBI:58349, ChEBI:CHEBI:59898;
CC Evidence={ECO:0000250|UniProtKB:Q6PHW0};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:27455;
CC Evidence={ECO:0000250|UniProtKB:Q6PHW0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-iodo-L-tyrosine + iodide + NADP(+) = 3,5-diiodo-L-tyrosine +
CC H(+) + NADPH; Xref=Rhea:RHEA:27457, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16382, ChEBI:CHEBI:57506, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:59898;
CC Evidence={ECO:0000269|PubMed:24153409};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:27459;
CC Evidence={ECO:0000269|PubMed:24153409};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=chloride + L-tyrosine + NADP(+) = 3-chloro-L-tyrosine + NADPH;
CC Xref=Rhea:RHEA:70343, ChEBI:CHEBI:17996, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58315, ChEBI:CHEBI:58349, ChEBI:CHEBI:189422;
CC Evidence={ECO:0000250|UniProtKB:Q6PHW0};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:70345;
CC Evidence={ECO:0000250|UniProtKB:Q6PHW0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=bromide + L-tyrosine + NADP(+) = 3-bromo-L-tyrosine + NADPH;
CC Xref=Rhea:RHEA:70347, ChEBI:CHEBI:15858, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58315, ChEBI:CHEBI:58349, ChEBI:CHEBI:189423;
CC Evidence={ECO:0000250|UniProtKB:Q6PHW0};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:70349;
CC Evidence={ECO:0000250|UniProtKB:Q6PHW0};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000269|PubMed:24153409};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=8 uM for diiodotyrosine (L-DIT) {ECO:0000269|PubMed:24153409};
CC Note=kcat 4.1 min(-1) for the deiodination of diiodotyrosine (L-DIT).
CC {ECO:0000269|PubMed:24153409};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the nitroreductase family. {ECO:0000305}.
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DR EMBL; CR450830; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001311483.1; NM_001324554.1.
DR AlphaFoldDB; E7FDV5; -.
DR SMR; E7FDV5; -.
DR STRING; 7955.ENSDARP00000101952; -.
DR PaxDb; E7FDV5; -.
DR Ensembl; ENSDART00000110282; ENSDARP00000101952; ENSDARG00000076056.
DR GeneID; 100330940; -.
DR KEGG; dre:100330940; -.
DR eggNOG; KOG3936; Eukaryota.
DR GeneTree; ENSGT00390000004348; -.
DR HOGENOM; CLU_070764_1_0_1; -.
DR InParanoid; E7FDV5; -.
DR OMA; WVDQDLQ; -.
DR OrthoDB; 1524590at2759; -.
DR PhylomeDB; E7FDV5; -.
DR TreeFam; TF313415; -.
DR Reactome; R-DRE-209968; Thyroxine biosynthesis.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 23.
DR Bgee; ENSDARG00000076056; Expressed in intestine and 5 other tissues.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0010181; F:FMN binding; IDA:UniProtKB.
DR GO; GO:0140616; F:iodotyrosine deiodinase activity; IDA:UniProtKB.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0006570; P:tyrosine metabolic process; IBA:GO_Central.
DR Gene3D; 3.40.109.10; -; 1.
DR InterPro; IPR029479; Nitroreductase.
DR InterPro; IPR000415; Nitroreductase-like.
DR Pfam; PF00881; Nitroreductase; 1.
DR SUPFAM; SSF55469; SSF55469; 1.
PE 1: Evidence at protein level;
KW Flavoprotein; FMN; Membrane; NADP; Oxidoreductase; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..295
FT /note="Iodotyrosine deiodinase"
FT /id="PRO_0000455639"
FT TRANSMEM 3..23
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 29..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..65
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 106..110
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q6PHW0"
FT BINDING 134..135
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q9DCX8"
FT BINDING 134
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q6PHW0"
FT BINDING 136
FT /ligand="3-iodo-L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:59898"
FT /evidence="ECO:0000250|UniProtKB:Q6PHW0"
FT BINDING 163
FT /ligand="3-iodo-L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:59898"
FT /evidence="ECO:0000250|UniProtKB:Q6PHW0"
FT BINDING 167
FT /ligand="3-iodo-L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:59898"
FT /evidence="ECO:0000250|UniProtKB:Q6PHW0"
FT BINDING 188
FT /ligand="3-iodo-L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:59898"
FT /evidence="ECO:0000250|UniProtKB:Q6PHW0"
FT BINDING 243..245
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q6PHW0"
FT BINDING 285
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q6PHW0"
SQ SEQUENCE 295 AA; 33685 MW; 971E673369131533 CRC64;
MAVFSSLTPV FVAVLCVIIG FLFKNSQRKE SRSKQKPSDQ TARPWVDEDL QDDTEISTKD
NEENNEDWMD TTDEENLPHV PYSPVQYSVS EMLDRSERFY TLMNLRRSVR FISPEPVPKE
VIDNVIRTAG TAPSGAHTEP WTFVVVSDTD VKHRIREIIE EEEEINYKQR MGNKWVQDLK
RLRTNWVKEY LDVAPYLILV FKQAYGILPS GKKKTHYYNE ISVSISCGIL LAALQNAGLV
TVTTTPLNCG PQLRSLLQRP ANEKLLMLLP VGFPASDAKV PDLKRKDLND IMVLV
