IYD1_PONAB
ID IYD1_PONAB Reviewed; 289 AA.
AC Q5REW1;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=Iodotyrosine deiodinase 1 {ECO:0000250|UniProtKB:Q6PHW0};
DE Short=IYD-1 {ECO:0000250|UniProtKB:Q6PHW0};
DE EC=1.21.1.1 {ECO:0000250|UniProtKB:Q6PHW0};
DE AltName: Full=Iodotyrosine dehalogenase 1 {ECO:0000250|UniProtKB:Q6PHW0};
GN Name=IYD; Synonyms=DEHAL1;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the dehalogenation of halotyrosines such as 3-
CC bromo-L-tyrosine, 3-chloro-L-tyrosine, 3-iodo-L-tyrosine and 3,5-
CC diiodo-L-tyrosine. During thyroid hormone biosynthesis, facilitates
CC iodide salvage by catalysing the oxidative NADPH-dependent deiodination
CC of the halogenated by-products of thyroid hormone production,
CC monoiodotyrosine (L-MIT) and diiodotyrosine (L-DIT). The scavanged
CC iodide can then reenter the hormone-producing pathways. Acts more
CC efficiently on 3-iodo-L-tyrosine than 3,5-diiodo-L-tyrosine.
CC {ECO:0000250|UniProtKB:Q6PHW0}.
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:0000250|UniProtKB:Q6PHW0};
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:0000250|UniProtKB:Q6PHW0};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:27459;
CC Evidence={ECO:0000250|UniProtKB:Q6PHW0};
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:0000250|UniProtKB:Q6PHW0};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q6PHW0}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q6PHW0};
CC Single-pass membrane protein {ECO:0000250|UniProtKB:Q6PHW0}.
CC Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:Q6PHW0}.
CC -!- SIMILARITY: Belongs to the nitroreductase family. {ECO:0000305}.
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DR EMBL; CR857405; CAH89696.1; -; mRNA.
DR RefSeq; NP_001124546.1; NM_001131074.1.
DR AlphaFoldDB; Q5REW1; -.
DR SMR; Q5REW1; -.
DR STRING; 9601.ENSPPYP00000019149; -.
DR GeneID; 100127058; -.
DR KEGG; pon:100127058; -.
DR CTD; 389434; -.
DR eggNOG; KOG3936; Eukaryota.
DR InParanoid; Q5REW1; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; ISS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0010181; F:FMN binding; ISS:UniProtKB.
DR GO; GO:0140616; F:iodotyrosine deiodinase activity; ISS:UniProtKB.
DR GO; GO:0042403; P:thyroid hormone metabolic process; ISS:UniProtKB.
DR GO; GO:0006570; P:tyrosine metabolic process; ISS:UniProtKB.
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 2: Evidence at transcript level;
KW Cell membrane; Cytoplasmic vesicle; Flavoprotein; FMN; Membrane; NADP;
KW Oxidoreductase; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..289
FT /note="Iodotyrosine deiodinase 1"
FT /id="PRO_0000230281"
FT TRANSMEM 1..21
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 47..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 100..104
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q6PHW0"
FT BINDING 128..129
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q9DCX8"
FT BINDING 128
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q6PHW0"
FT BINDING 130
FT /ligand="3,5-diiodo-L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:57506"
FT /evidence="ECO:0000250|UniProtKB:Q9DCX8"
FT BINDING 130
FT /ligand="3-iodo-L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:59898"
FT /evidence="ECO:0000250|UniProtKB:Q9DCX8"
FT BINDING 157
FT /ligand="3,5-diiodo-L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:57506"
FT /evidence="ECO:0000250|UniProtKB:Q9DCX8"
FT BINDING 157
FT /ligand="3-iodo-L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:59898"
FT /evidence="ECO:0000250|UniProtKB:Q9DCX8"
FT BINDING 161
FT /ligand="3,5-diiodo-L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:57506"
FT /evidence="ECO:0000250|UniProtKB:Q9DCX8"
FT BINDING 161
FT /ligand="3-iodo-L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:59898"
FT /evidence="ECO:0000250|UniProtKB:Q9DCX8"
FT BINDING 182
FT /ligand="3,5-diiodo-L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:57506"
FT /evidence="ECO:0000250|UniProtKB:Q9DCX8"
FT BINDING 182
FT /ligand="3-iodo-L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:59898"
FT /evidence="ECO:0000250|UniProtKB:Q9DCX8"
FT BINDING 237..239
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q6PHW0"
FT BINDING 279
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q6PHW0"
SQ SEQUENCE 289 AA; 33365 MW; F298872E6751DF7F CRC64;
MYFLTPILVA ILCILVVWIF KNADRSMEKK KGEARTRAEA RPWVDEDLKD SSDLHQAEED
ADEWQESEEN VEHIPFSHTH YPEKEMVKRS REFYELLNKR RSVRFISNEQ VPMEVIDNVI
RTAGTAPSGA HTEPWTFVVV KDPDVKHKIR KIIEGEEEIN YMKRMGHRWV TDLKKLRTNW
IKEYLDTAPI LILIFKQVHG FVANGKKKVH YYNEISVSIA CGILLAALQN AGLVTVTTTP
LNCGPRLRVL LGRPAHEKLL MLLPVGYPSK EAMVPDLKRK PLDQIMVMV
