ID   TY3H_ANGAN              Reviewed;         488 AA.
AC   O42091;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 96.
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   Anguilla anguilla (European freshwater eel) (Muraena anguilla).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Anguilliformes; Anguillidae;
OC   Anguilla.
OX   NCBI_TaxID=7936;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=9681435; DOI=10.1046/j.1471-4159.1998.71020460.x;
RA   Boularand S., Biguet N.F., Vidal B., Veron M., Mallet J., Vincent J.D.,
RA   Dufour S., Vernier P.;
RT   "Tyrosine hydroxylase in the European eel (Anguilla anguilla): cDNA
RT   cloning, brain distribution, and phylogenetic analysis.";
RL   J. Neurochem. 71:460-470(1998).
CC   -!- FUNCTION: Plays an important role in the physiology of adrenergic
CC       neurons. {ECO:0000250}.
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   -!- ACTIVITY REGULATION: Phosphorylation leads to an increase in the
CC       catalytic activity. {ECO:0000250|UniProtKB:P07101}.
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}. Cell projection, axon
CC       {ECO:0000250|UniProtKB:P24529}. Note=Expressed in dopaminergic axons
CC       and axon terminals. {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; AJ000731; CAA04264.1; -; mRNA.
DR   AlphaFoldDB; O42091; -.
DR   SMR; O42091; -.
DR   OMA; PELDMNH; -.
DR   UniPathway; UPA00747; UER00733.
DR   GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
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 family metabolic process; IEA:InterPro.
DR   GO; GO:0042416; P:dopamine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0042136; P:neurotransmitter biosynthetic process; IEA:UniProtKB-KW.
DR   CDD; cd03345; eu_TyrOH; 1.
DR   Gene3D; 1.10.800.10; -; 1.
DR   InterPro; IPR045865; ACT-like_dom_sf.
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   InterPro; IPR021164; Tyrosine_hydroxylase_CS.
DR   PANTHER; PTHR11473; PTHR11473; 1.
DR   Pfam; PF00351; Biopterin_H; 1.
DR   Pfam; PF12549; TOH_N; 1.
DR   PIRSF; PIRSF000336; TH; 1.
DR   PRINTS; PR00372; FYWHYDRXLASE.
DR   SUPFAM; SSF55021; SSF55021; 1.
DR   SUPFAM; SSF56534; SSF56534; 1.
DR   TIGRFAMs; TIGR01269; Tyr_3_monoox; 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; Cell projection; Cytoplasm; Iron;
KW   Metal-binding; Monooxygenase; Neurotransmitter biosynthesis;
KW   Oxidoreductase; Phosphoprotein.
FT   CHAIN           1..488
FT                   /note="Tyrosine 3-monooxygenase"
FT                   /id="PRO_0000205559"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..17
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         321
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         326
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         366
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         38
FT                   /note="Phosphoserine; by PKA"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   488 AA;  55490 MW;  573553BA39EBD448 CRC64;
     MPISNSSGSS TKSITRAGSE LDRADSITSP RFVGRRQSLI EDARKEREAA AAAESSEASE
     QIVFDEEDGK ALLNLFFTLR SSKIPALSRA LKVFETFEAK IHHLETRTRR KPKDSLEDLE
     YFVRCEVHLA DVSTLISSIR RIAEDVRTTK EVKFHWFPKK ISELDSCHHL VTKFDPDLDQ
     DHPGFTDPVY RQRRRMIGEI AFRYKHGEPI PRVEYTEEEI GTWREVYSTL RDLYTTHACS
     EHLEAFRLLE RHCGYSPNSI PQLEDVSHFL KERTGFQLRP VAGLLSARDF LASLAFRVFQ
     CTQYIRHASS PMHSPEPDCV HELLGHVPML ADRTFAQFSQ NIGLASLGAS EEDIEKLSTL
     YWFTVEFGLC KQGDGVKAYG AGLLSSYGEL VHSLSDEPER REFDPEAAAA EPYQDQNYQS
     VYFVSESFTD AKEKLRVYAA GINRPFSVRF DPYTYSIEVL DNPLKIRGGL ESVKDELKVL
     TDALNVLA