ID   TY3H_SCHMA              Reviewed;         465 AA.
AC   O17446;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   24-JAN-2024, entry version 98.
DE   RecName: Full=Tyrosine 3-monooxygenase;
DE            EC=1.14.16.2;
DE   AltName: Full=Tyrosine 3-hydroxylase;
DE            Short=TH;
GN   Name=TH;
OS   Schistosoma mansoni (Blood fluke).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC   Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX   NCBI_TaxID=6183;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Puerto Rican;
RX   PubMed=9751167; DOI=10.1046/j.1471-4159.1998.71041369.x;
RA   Hamdan F.F., Ribeiro P.;
RT   "Cloning and characterization of a novel form of tyrosine hydroxylase from
RT   the human parasite, Schistosoma mansoni.";
RL   J. Neurochem. 71:1369-1380(1998).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin + L-tyrosine + O2 =
CC         (4aS,6R)-4a-hydroxy-L-erythro-5,6,7,8-tetrahydrobiopterin + L-dopa;
CC         Xref=Rhea:RHEA:18201, ChEBI:CHEBI:15379, ChEBI:CHEBI:15642,
CC         ChEBI:CHEBI:57504, ChEBI:CHEBI:58315, ChEBI:CHEBI:59560;
CC         EC=1.14.16.2;
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC   -!- PATHWAY: Catecholamine biosynthesis; dopamine biosynthesis; dopamine
CC       from L-tyrosine: step 1/2.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region
CC       {ECO:0000250|UniProtKB:P24529}.
CC   -!- SIMILARITY: Belongs to the biopterin-dependent aromatic amino acid
CC       hydroxylase family. {ECO:0000305}.
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DR   EMBL; AF030336; AAC62256.1; -; mRNA.
DR   AlphaFoldDB; O17446; -.
DR   SMR; O17446; -.
DR   STRING; 6183.O17446; -.
DR   InParanoid; O17446; -.
DR   UniPathway; UPA00747; UER00733.
DR   Proteomes; UP000008854; Unassembled WGS sequence.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0004511; F:tyrosine 3-monooxygenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009072; P:aromatic amino acid metabolic process; IEA:InterPro.
DR   GO; GO:0042416; P:dopamine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd03345; eu_TyrOH; 1.
DR   Gene3D; 1.10.800.10; Aromatic amino acid hydroxylase; 1.
DR   InterPro; IPR001273; ArAA_hydroxylase.
DR   InterPro; IPR018301; ArAA_hydroxylase_Fe/CU_BS.
DR   InterPro; IPR036951; ArAA_hydroxylase_sf.
DR   InterPro; IPR036329; Aro-AA_hydroxylase_C_sf.
DR   InterPro; IPR019774; Aromatic-AA_hydroxylase_C.
DR   InterPro; IPR041903; Eu_TyrOH_cat.
DR   InterPro; IPR005962; Tyr_3_mOase.
DR   InterPro; IPR019773; Tyrosine_3-monooxygenase-like.
DR   NCBIfam; TIGR01269; Tyr_3_monoox; 1.
DR   PANTHER; PTHR11473; AROMATIC AMINO ACID HYDROXYLASE; 1.
DR   PANTHER; PTHR11473:SF15; TYROSINE 3-MONOOXYGENASE; 1.
DR   Pfam; PF00351; Biopterin_H; 1.
DR   PIRSF; PIRSF000336; TH; 1.
DR   PRINTS; PR00372; FYWHYDRXLASE.
DR   SUPFAM; SSF56534; Aromatic aminoacid monoxygenases, catalytic and oligomerization domains; 1.
DR   PROSITE; PS00367; BH4_AAA_HYDROXYL_1; 1.
DR   PROSITE; PS51410; BH4_AAA_HYDROXYL_2; 1.
PE   2: Evidence at transcript level;
KW   Catecholamine biosynthesis; Cytoplasm; Iron; Metal-binding; Monooxygenase;
KW   Neurotransmitter biosynthesis; Oxidoreductase; Reference proteome.
FT   CHAIN           1..465
FT                   /note="Tyrosine 3-monooxygenase"
FT                   /id="PRO_0000205567"
FT   BINDING         294
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         299
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         339
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   465 AA;  54081 MW;  0DE47B4A474665CB CRC64;
     MKMTMMCDES IEENNKSSTV ELNHNEKDGR IHSIIINFHP ITHEQSNNQF YIQTLHEILK
     YIIDKKLNLV HFETRPTLTL SNANRDVQYS CLITLEANEI NMSLLYEELR GNSFISGINL
     LNNQESEDWY PKHISDLDKC QHLLRKFQPE LQTDHPGFHD KVYRERREAI AKIAFQYKYG
     DRIPEVEYTK EEIETWGLVF TKMKAVHASR ACREYIDGFQ LLEKYCNYNS ESIPQLQTIC
     EFMHRTSGFR IRPVAGLVSP KDFLASLAFR VFQCTQYIRH HSRPMHTPEP DCIHELIGHM
     PMLVNRQFAD FSQELGLASL GASEEEITRL STLYWFTVEF GLCNENGETR ALGAGIMSSY
     GELENAFSDL SVKEPFNIND AAVQVYDDVG YQKIYFVTES IESMKRELRN YINTSGKSTI
     PIYDPITETV HMKSRFSIRK ELLKHVKEEI GQLDTLLNHS NYTLP
//