IYD_HALH1
ID IYD_HALH1 Reviewed; 222 AA.
AC F4KU78;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 58.
DE RecName: Full=Iodotyrosine deiodinase {ECO:0000303|PubMed:24153409};
DE EC=1.21.1.1 {ECO:0000269|PubMed:24153409, ECO:0000269|PubMed:28157283};
DE AltName: Full=Halotyrosine dehalogenase {ECO:0000305|PubMed:28157283};
GN Name=IYD {ECO:0000303|PubMed:24153409};
GN OrderedLocusNames=Halhy_2296 {ECO:0000312|EMBL:AEE50175.1};
OS Haliscomenobacter hydrossis (strain ATCC 27775 / DSM 1100 / LMG 10767 / O).
OC Bacteria; Bacteroidetes; Saprospiria; Saprospirales;
OC Haliscomenobacteraceae; Haliscomenobacter.
OX NCBI_TaxID=760192 {ECO:0000312|Proteomes:UP000008461};
RN [1] {ECO:0000312|Proteomes:UP000008461}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27775 / DSM 1100 / LMG 10767 / O
RC {ECO:0000312|Proteomes:UP000008461};
RX PubMed=21886862; DOI=10.4056/sigs.1964579;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Daligault H., Lapidus A., Zeytun A., Nolan M., Lucas S., Del Rio T.G.,
RA Tice H., Cheng J.F., Tapia R., Han C., Goodwin L., Pitluck S., Liolios K.,
RA Pagani I., Ivanova N., Huntemann M., Mavromatis K., Mikhailova N., Pati A.,
RA Chen A., Palaniappan K., Land M., Hauser L., Brambilla E.M., Rohde M.,
RA Verbarg S., Goker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P., Woyke T.;
RT "Complete genome sequence of Haliscomenobacter hydrossis type strain (O).";
RL Stand. Genomic Sci. 4:352-360(2011).
RN [2] {ECO:0000312|Proteomes:UP000008461}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27775 / DSM 1100 / LMG 10767 / O {ECO:0000303|Ref.2};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Han J., Lapidus A., Bruce D., Goodwin L., Pitluck S., Peters L.,
RA Kyrpides N., Mavromatis K., Ivanova N., Ovchinnikova G., Pagani I.,
RA Daligault H., Detter J.C., Han C., Land M., Hauser L., Markowitz V.,
RA Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Verbarg S., Frueling A.,
RA Brambilla E., Klenk H.-P., Eisen J.A.;
RT "Complete sequence of chromosome of Haliscomenobacter hydrossis DSM 1100.";
RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND COFACTOR.
RC STRAIN=ATCC 27775 / DSM 1100 / LMG 10767 / O {ECO:0000303|PubMed:24153409};
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).
RN [4] {ECO:0007744|PDB:5KO7, ECO:0007744|PDB:5KO8, ECO:0007744|PDB:5KRD}
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH FMN AND
RP 3-IODO-L-TYROSINE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, COFACTOR, AND SUBUNIT.
RC STRAIN=ATCC 27775 / DSM 1100 / LMG 10767 / O {ECO:0000303|PubMed:28157283};
RX PubMed=28157283; DOI=10.1021/acs.biochem.6b01308;
RA Ingavat N., Kavran J.M., Sun Z., Rokita S.E.;
RT "Active Site Binding Is Not Sufficient for Reductive Deiodination by
RT Iodotyrosine Deiodinase.";
RL Biochemistry 56:1130-1139(2017).
CC -!- FUNCTION: Catalyzes the dehalogenation of halotyrosines such as 3-iodo-
CC L-tyrosine and 3,5-diiodo-L-tyrosine (PubMed:24153409,
CC PubMed:28157283). Likely to also catalyze the dehalogenation of other
CC halotyrosines such as 3-bromo-L-tyrosine, 3-chloro-L-tyrosine and 3-
CC iodo-L-tyrosine (By similarity). Activity towards 3-iodo-L-tyrosine is
CC much stronger than activity towards 3,5-diiodo-L-tyrosine and 2-
CC iodophenol (PubMed:28157283, PubMed:24153409).
CC {ECO:0000250|UniProtKB:B9K712, ECO:0000269|PubMed:24153409,
CC ECO:0000269|PubMed:28157283}.
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, ECO:0000269|PubMed:28157283};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:32481;
CC Evidence={ECO:0000269|PubMed:24153409, ECO:0000269|PubMed:28157283};
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:0000269|PubMed:28157283};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:27455;
CC Evidence={ECO:0000269|PubMed:28157283};
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, ECO:0000269|PubMed:28157283};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:27459;
CC Evidence={ECO:0000269|PubMed:24153409, ECO:0000269|PubMed:28157283};
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:B9K712};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:70345;
CC Evidence={ECO:0000250|UniProtKB:B9K712};
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:B9K712};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:70349;
CC Evidence={ECO:0000250|UniProtKB:B9K712};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000269|PubMed:24153409, ECO:0000269|PubMed:28157283};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=6.6 uM for 3,5-diiodo-L-tyrosine {ECO:0000269|PubMed:24153409};
CC KM=0.012 mM for 3-iodo-L-tyrosine (at pH 7.4 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:28157283};
CC KM=4.1 mM for 2-iodophenol (at pH 7.4 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:28157283};
CC Note=kcat 0.09 sec(-1) for the deiodination of 3,5-diiodo-L-tyrosine
CC (PubMed:24153409). kcat is 0.27 sec(-1) for the dehalogenation of 3-
CC iodo-L-tyrosine (at pH 7.4 and 25 degrees Celsius) (PubMed:28157283).
CC kcat is 0.0029 sec(-1) for the dehalogenation of 2-iodophenol (at pH
CC 7.4 and 25 degrees Celsius) (PubMed:28157283).
CC {ECO:0000269|PubMed:24153409, ECO:0000269|PubMed:28157283};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:28157283}.
CC -!- SIMILARITY: Belongs to the nitroreductase family. {ECO:0000305}.
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DR EMBL; CP002691; AEE50175.1; -; Genomic_DNA.
DR RefSeq; WP_013764725.1; NC_015510.1.
DR PDB; 5KO7; X-ray; 2.25 A; A/B=1-222.
DR PDB; 5KO8; X-ray; 2.15 A; A/B=1-222.
DR PDB; 5KRD; X-ray; 2.10 A; A/B=1-222.
DR PDBsum; 5KO7; -.
DR PDBsum; 5KO8; -.
DR PDBsum; 5KRD; -.
DR SMR; F4KU78; -.
DR STRING; 760192.Halhy_2296; -.
DR EnsemblBacteria; AEE50175; AEE50175; Halhy_2296.
DR KEGG; hhy:Halhy_2296; -.
DR eggNOG; COG0778; Bacteria.
DR HOGENOM; CLU_070764_1_0_10; -.
DR OMA; WVDQDLQ; -.
DR OrthoDB; 1847197at2; -.
DR BRENDA; 1.21.1.1; 2681.
DR Proteomes; UP000008461; Chromosome.
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 3D-structure; Flavoprotein; FMN; NADP; Nucleotide-binding; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..222
FT /note="Iodotyrosine deiodinase"
FT /id="PRO_0000455638"
FT BINDING 34..38
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:28157283,
FT ECO:0007744|PDB:5KO7, ECO:0007744|PDB:5KO8,
FT ECO:0007744|PDB:5KRD"
FT BINDING 61..62
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:28157283,
FT ECO:0007744|PDB:5KO8, ECO:0007744|PDB:5KRD"
FT BINDING 91
FT /ligand="3-iodo-L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:59898"
FT /evidence="ECO:0000269|PubMed:28157283,
FT ECO:0007744|PDB:5KO8"
FT BINDING 95
FT /ligand="3-iodo-L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:59898"
FT /evidence="ECO:0000269|PubMed:28157283,
FT ECO:0007744|PDB:5KO8"
FT BINDING 116
FT /ligand="3-iodo-L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:59898"
FT /evidence="ECO:0000269|PubMed:28157283,
FT ECO:0007744|PDB:5KO8"
FT BINDING 171..173
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:28157283,
FT ECO:0007744|PDB:5KO7, ECO:0007744|PDB:5KO8,
FT ECO:0007744|PDB:5KRD"
FT BINDING 212
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:28157283,
FT ECO:0007744|PDB:5KO7, ECO:0007744|PDB:5KO8,
FT ECO:0007744|PDB:5KRD"
SQ SEQUENCE 222 AA; 25308 MW; 514FBB2F3D51C0ED CRC64;
MKQKPAFIPY AGAQFEPEEM LSKSAEYYQF MDHRRTVREF SNRAIPLEVI ENIVMTASTA
PSGAHKQPWT FVVVSDPQIK AKIRQAAEKE EFESYNGRMS NEWLEDLQPF GTDWHKPFLE
IAPYLIVVFR KAYDVLPDGT QRKNYYVQES VGIACGFLLA AIHQAGLVAL THTPSPMNFL
QKILQRPENE RPFLLVPVGY PAEGAMVPDL QRKDKAAVMV VY
