IYD_DAPPU
ID IYD_DAPPU Reviewed; 300 AA.
AC E9FR69;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 1.
DT 03-AUG-2022, entry version 44.
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 ORFNames=DAPPUDRAFT_205384 {ECO:0000312|EMBL:EFX90111.1};
OS Daphnia pulex (Water flea).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Branchiopoda;
OC Diplostraca; Cladocera; Anomopoda; Daphniidae; Daphnia.
OX NCBI_TaxID=6669 {ECO:0000312|Proteomes:UP000000305};
RN [1] {ECO:0000312|Proteomes:UP000000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21292972; DOI=10.1126/science.1197761;
RA Colbourne J.K., Pfrender M.E., Gilbert D., Thomas W.K., Tucker A.,
RA Oakley T.H., Tokishita S., Aerts A., Arnold G.J., Basu M.K., Bauer D.J.,
RA Caceres C.E., Carmel L., Casola C., Choi J.H., Detter J.C., Dong Q.,
RA Dusheyko S., Eads B.D., Frohlich T., Geiler-Samerotte K.A., Gerlach D.,
RA Hatcher P., Jogdeo S., Krijgsveld J., Kriventseva E.V., Kultz D.,
RA Laforsch C., Lindquist E., Lopez J., Manak J.R., Muller J., Pangilinan J.,
RA Patwardhan R.P., Pitluck S., Pritham E.J., Rechtsteiner A., Rho M.,
RA Rogozin I.B., Sakarya O., Salamov A., Schaack S., Shapiro H., Shiga Y.,
RA Skalitzky C., Smith Z., Souvorov A., Sung W., Tang Z., Tsuchiya D., Tu H.,
RA Vos H., Wang M., Wolf Y.I., Yamagata H., Yamada T., Ye Y., Shaw J.R.,
RA Andrews J., Crease T.J., Tang H., Lucas S.M., Robertson H.M., Bork P.,
RA Koonin E.V., Zdobnov E.M., Grigoriev I.V., Lynch M., Boore J.L.;
RT "The ecoresponsive genome of Daphnia pulex.";
RL Science 331:555-561(2011).
RN [2] {ECO:0000305}
RP PARTIAL PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, PROTEOLYTIC
RP CLEAVAGE, 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:0000250|UniProtKB:E1JIB2};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=7 uM for diiodotyrosine (L-DIT) {ECO:0000269|PubMed:24153409};
CC Note=Kcat 17.6 min(-1) for the deiodination of diiodotyrosine (L-
CC DIT). {ECO:0000269|PubMed:24153409};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- PTM: May be cleaved at Gln-55 (PubMed:24153409). The cleaved form
CC retains catalytic activity (PubMed:24153409).
CC {ECO:0000269|PubMed:24153409}.
CC -!- SIMILARITY: Belongs to the nitroreductase family. {ECO:0000305}.
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DR EMBL; GL732523; EFX90111.1; -; Genomic_DNA.
DR STRING; 6669.EFX90111; -.
DR EnsemblMetazoa; EFX90111; EFX90111; DAPPUDRAFT_205384.
DR KEGG; dpx:DAPPUDRAFT_205384; -.
DR eggNOG; KOG3936; Eukaryota.
DR HOGENOM; CLU_070764_1_0_1; -.
DR InParanoid; E9FR69; -.
DR OMA; WVDQDLQ; -.
DR OrthoDB; 1524590at2759; -.
DR PhylomeDB; E9FR69; -.
DR Proteomes; UP000000305; Unassembled WGS sequence.
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 Direct protein sequencing; Flavoprotein; FMN; Membrane; NADP;
KW Oxidoreductase; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..300
FT /note="Iodotyrosine deiodinase"
FT /id="PRO_0000455640"
FT TRANSMEM 15..31
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 110..114
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q6PHW0"
FT BINDING 138..139
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q9DCX8"
FT BINDING 138
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q6PHW0"
FT BINDING 140
FT /ligand="3,5-diiodo-L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:57506"
FT /evidence="ECO:0000250|UniProtKB:Q9DCX8"
FT BINDING 140
FT /ligand="3-iodo-L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:59898"
FT /evidence="ECO:0000250|UniProtKB:Q9DCX8"
FT BINDING 167
FT /ligand="3,5-diiodo-L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:57506"
FT /evidence="ECO:0000250|UniProtKB:E1JIB2"
FT BINDING 167
FT /ligand="3-iodo-L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:59898"
FT /evidence="ECO:0000250|UniProtKB:E1JIB2"
FT BINDING 171
FT /ligand="3,5-diiodo-L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:57506"
FT /evidence="ECO:0000250|UniProtKB:E1JIB2"
FT BINDING 171
FT /ligand="3-iodo-L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:59898"
FT /evidence="ECO:0000250|UniProtKB:E1JIB2"
FT BINDING 192
FT /ligand="3,5-diiodo-L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:57506"
FT /evidence="ECO:0000250|UniProtKB:E1JIB2"
FT BINDING 192
FT /ligand="3-iodo-L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:59898"
FT /evidence="ECO:0000250|UniProtKB:E1JIB2"
FT BINDING 247..249
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q6PHW0"
FT BINDING 289
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q6PHW0"
SQ SEQUENCE 300 AA; 34084 MW; B0B06853726ACCB4 CRC64;
MENYVPFLVS HWRTVGLISV SIAAGVALGQ LNQTHERAAN KSQRVHTNSS IKAKQVKRES
AIEQINEIED DDEQSLEDQD VLPILFQYEK PSEADSIRRS EEFYRRMNQR RSVREISSDP
VALEVIENII KTGGTSPSGA HTEPWTFVVV SNLEMKQQIR QIIEAEEEIN YKQRMGDVWV
QDLQPVGTTW VKEYLTEAPW LILIFKQVHG FKRNGQKKIH YYNEISVSIA TGFLLAAIQE
AGLVTVTTTP LNCGPSIRVL LGRPVNEKLL LLLPVGYPKV GATVPDFKRK PLHDIMVHYQ
