IYD_HYDVU
ID IYD_HYDVU Reviewed; 272 AA.
AC T2MBC4;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2013, sequence version 1.
DT 03-AUG-2022, entry version 27.
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 {ECO:0000312|EMBL:CDG69386.1};
GN Synonyms=LOC100199794 {ECO:0000312|RefSeq:XP_002164528.2};
OS Hydra vulgaris (Hydra) (Hydra attenuata).
OC Eukaryota; Metazoa; Cnidaria; Hydrozoa; Hydroidolina; Anthoathecata;
OC Aplanulata; Hydridae; Hydra.
OX NCBI_TaxID=6087 {ECO:0000312|EMBL:CDG69386.1};
RN [1] {ECO:0000312|EMBL:CDG69386.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Wenger Y.;
RL Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases.
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=4 uM for diiodotyrosine (L-DIT) {ECO:0000269|PubMed:24153409};
CC Note=Kcat 14 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; HAAD01003154; CDG69386.1; -; mRNA.
DR RefSeq; XP_002164528.2; XM_002164492.3.
DR GeneID; 100199794; -.
DR KEGG; hmg:100199794; -.
DR OMA; WVDQDLQ; -.
DR OrthoDB; 1524590at2759; -.
DR Proteomes; UP000694840; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0010181; F:FMN binding; IDA:UniProtKB.
DR GO; GO:0140616; F:iodotyrosine deiodinase activity; IDA: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 1: Evidence at protein level;
KW Flavoprotein; FMN; Membrane; NADP; Oxidoreductase; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..272
FT /note="Iodotyrosine deiodinase"
FT /id="PRO_0000455641"
FT TRANSMEM 5..25
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 82..86
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q6PHW0"
FT BINDING 110..111
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q9DCX8"
FT BINDING 110
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q6PHW0"
FT BINDING 112
FT /ligand="3-iodo-L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:59898"
FT /evidence="ECO:0000250|UniProtKB:Q6PHW0"
FT BINDING 139
FT /ligand="3-iodo-L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:59898"
FT /evidence="ECO:0000250|UniProtKB:Q6PHW0"
FT BINDING 143
FT /ligand="3-iodo-L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:59898"
FT /evidence="ECO:0000250|UniProtKB:Q6PHW0"
FT BINDING 164
FT /ligand="3-iodo-L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:59898"
FT /evidence="ECO:0000250|UniProtKB:Q6PHW0"
FT BINDING 219..221
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q6PHW0"
FT BINDING 261
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q6PHW0"
SQ SEQUENCE 272 AA; 31256 MW; 3F2F9A6D7B374BF2 CRC64;
MFDNLSGVSY GLLAGILAML IHLVYQKITE LKRRKDELKE RESHPTDDLF PKEDFIPYHP
SRYSEEEMIK RSNDFYLSMN ARRSVRFFSN EDVPDEVIDN IIRTAGTSPS GAHTEPWTFV
VIKNKLLKAK VREIIEEEEE LNYKQRMGQK WVDDLKPLKT NWIKEYLTEA PYLILVFKQT
YGITEDGQKK THYYNEISAS ISCGFLLAAI QNAGLVALTS TPLNAGSKLR NLVGRGPNEK
IVILLPVGYP SKNCQVPNLK RKPLNEIMIK FD
