Detail Information for IndEnz0018000714
IED ID IndEnz0018000714
Enzyme Type ID peroxidase000714
Protein Name Thyroid peroxidase
TPO
EC 1.11.1.8
Gene Name TPO
Organism Sus scrofa (Pig)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Laurasiatheria Artiodactyla Suina Suidae (pigs) Sus Sus scrofa (Pig)
Enzyme Sequence MGARAVLGVTLAVACAGAFFASILRRKDLLGGDTEASGVAGLVEASRLLVDEAIHTTMRRNLRKRGIFSPSQLLSFSKLPEPTSRTASRAAEIMETAVQEVKRRVCRRRDTDQLPTDVLSEELLSTIANLSGCLPHMLPPSCPHTCLANKYRLITGACNNRDHPRWGASNTALARWLPPAYEDGVTEPRGWNPHFLYNGLPLPPVREVTRQVIHVSNEAVTEDGQYSDLLMAWGQYIDHDIAFTPQSTSKAAFAGGADCQLTCENRSPCFPIQLPTNASGAAGATCLPFYRSSAACGSGRQGALVGNLSWAAPRQQMNGLTSFLDASTVYGSSPAQEQRLRNWTSAEGLLRVNTRHRDAGRAFLPFAPPPAPPACAPEPGTPAARAPCFLAGDSRASEVPGLTALHTLWLREHNRLAAAFKALNAHWSADTVYQEARKVVGALHQIVTLRDYVPKILGAEAFGQHVGPYQGYDPAVDPTVSNVFSTAAFRFGHATIHPLVRRLDARFQEHPGSHLPLRAAFFQPWRLLREGGVDPVLRGLLARPAKLQVQDQLMNEELTERLFVLSNSGTLDLASINLQRGRDHGLPGYNEWREFCGLSRLETWADLSAATANGRVADRILGLYQHPDNIDVWLGGLAESFLPGARTGPLFACIIGKQMRALRDGDRFWWENPGVFTEAQRRELSRHSMSRVICDNSGLSHVPLDAFRVGQWPQEFEPCASIQGMDLGAWREAPPSGDACGFPDPVEDGGFLLCEERGQRVLVFSCRHGFRLRGPAQITCTPRGWDSPPPLCKDINECEDETDPPCHASARCKNTKGGVLCECSDPLVLGEDGRTCVDAGRLPRASVVSIALGAVLVCGLAGLAWTVVCRWTHADARPLLPVGEGEGDGKSPSLPLPGCGNRRDVGAAPALEVEQDLSCGSRGLCE
Enzyme Length 926
Uniprot Accession Number P09933
Absorption
Active Site ACT_SITE 239; /note=Proton acceptor; /evidence=ECO:0000255|PROSITE-ProRule:PRU00298
Activity Regulation
Binding Site BINDING 238; /note="Heme b; covalent, via 2 links"; /evidence="ECO:0000250"; BINDING 398; /note="Heme b; covalent, via 2 links"; /evidence="ECO:0000250"
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=2 H(+) + H2O2 + 2 iodide = diiodine + 2 H2O; Xref=Rhea:RHEA:23336, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16240, ChEBI:CHEBI:16382, ChEBI:CHEBI:17606; EC=1.11.1.8; Evidence={ECO:0000269|PubMed:12325367, ECO:0000269|PubMed:2996435, ECO:0000269|PubMed:7142155}; CATALYTIC ACTIVITY: Reaction=[thyroglobulin]-L-tyrosine + H(+) + H2O2 + iodide = [thyroglobulin]-3-iodo-L-tyrosine + 2 H2O; Xref=Rhea:RHEA:48956, Rhea:RHEA-COMP:12274, Rhea:RHEA-COMP:12275, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16240, ChEBI:CHEBI:16382, ChEBI:CHEBI:46858, ChEBI:CHEBI:90870; EC=1.11.1.8; Evidence={ECO:0000269|PubMed:12325367, ECO:0000269|PubMed:2996435, ECO:0000269|PubMed:7142155}; CATALYTIC ACTIVITY: Reaction=[thyroglobulin]-3-iodo-L-tyrosine + H(+) + H2O2 + iodide = [thyroglobulin]-3,5-diiodo-L-tyrosine + 2 H2O; Xref=Rhea:RHEA:48960, Rhea:RHEA-COMP:12275, Rhea:RHEA-COMP:12276, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16240, ChEBI:CHEBI:16382, ChEBI:CHEBI:90870, ChEBI:CHEBI:90871; EC=1.11.1.8; Evidence={ECO:0000269|PubMed:12325367, ECO:0000269|PubMed:2996435, ECO:0000269|PubMed:7142155}; CATALYTIC ACTIVITY: Reaction=2 [thyroglobulin]-3,5-diiodo-L-tyrosine + H2O2 = [thyroglobulin]-dehydroalanine + [thyroglobulin]-L-thyroxine + 2 H2O; Xref=Rhea:RHEA:48964, Rhea:RHEA-COMP:12276, Rhea:RHEA-COMP:12277, Rhea:RHEA-COMP:12278, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240, ChEBI:CHEBI:90871, ChEBI:CHEBI:90872, ChEBI:CHEBI:90873; EC=1.11.1.8; Evidence={ECO:0000269|PubMed:12325367, ECO:0000269|PubMed:2996435, ECO:0000269|PubMed:7142155}; CATALYTIC ACTIVITY: Reaction=[thyroglobulin]-3,5-diiodo-L-tyrosine + [thyroglobulin]-3-iodo-L-tyrosine + H2O2 = [thyroglobulin]-3,3',5-triiodo-L-thyronine + [thyroglobulin]-dehydroalanine + 2 H2O; Xref=Rhea:RHEA:48968, Rhea:RHEA-COMP:12275, Rhea:RHEA-COMP:12276, Rhea:RHEA-COMP:12278, Rhea:RHEA-COMP:12279, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240, ChEBI:CHEBI:90870, ChEBI:CHEBI:90871, ChEBI:CHEBI:90873, ChEBI:CHEBI:90874; EC=1.11.1.8; Evidence={ECO:0000269|PubMed:12325367, ECO:0000269|PubMed:2996435, ECO:0000269|PubMed:7142155};
DNA Binding
EC Number 1.11.1.8
Enzyme Function FUNCTION: Iodination and coupling of the hormonogenic tyrosines in thyroglobulin to yield the thyroid hormones T(3) and T(4). {ECO:0000269|PubMed:12325367, ECO:0000269|PubMed:2996435}.
Temperature Dependency
PH Dependency
Pathway PATHWAY: Hormone biosynthesis; thyroid hormone biosynthesis.
nucleotide Binding
Features Active site (1); Binding site (2); Chain (1); Disulfide bond (10); Domain (2); Glycosylation (4); Metal binding (6); Signal peptide (1); Site (1); Topological domain (2); Transmembrane (1)
Keywords Calcium;Direct protein sequencing;Disulfide bond;EGF-like domain;Glycoprotein;Heme;Hydrogen peroxide;Iron;Membrane;Metal-binding;Oxidoreductase;Peroxidase;Reference proteome;Signal;Sushi;Thyroid hormones biosynthesis;Transmembrane;Transmembrane helix
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
Modified Residue
Post Translational Modification PTM: Heme is covalently bound through a H(2)O(2)-dependent autocatalytic process. Heme insertion is important for the delivery of protein at the cell surface (By similarity). {ECO:0000250}.; PTM: Cleaved in its N-terminal part. {ECO:0000250}.; PTM: N-glycosylated; contains mannose and N-acetylglucosamine. {ECO:0000269|PubMed:1497352}.
Signal Peptide SIGNAL 1..14; /evidence=ECO:0000255
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 100,443
Kinetics
Metal Binding METAL 240; /note=Calcium; /evidence=ECO:0000255|PROSITE-ProRule:PRU00298; METAL 321; /note=Calcium; /evidence=ECO:0000255|PROSITE-ProRule:PRU00298; METAL 323; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000255|PROSITE-ProRule:PRU00298; METAL 325; /note=Calcium; /evidence=ECO:0000255|PROSITE-ProRule:PRU00298; METAL 327; /note=Calcium; /evidence=ECO:0000255|PROSITE-ProRule:PRU00298; METAL 493; /note=Iron (heme b axial ligand); /evidence=ECO:0000255|PROSITE-ProRule:PRU00298
Rhea ID RHEA:23336; RHEA:48956; RHEA:48960; RHEA:48964; RHEA:48968
Cross Reference Brenda 1.11.1.8;