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Database: UniProt
Entry: A0A7J7QTI3_MYOMY
LinkDB: A0A7J7QTI3_MYOMY
Original site: A0A7J7QTI3_MYOMY 
ID   A0A7J7QTI3_MYOMY        Unreviewed;       474 AA.
AC   A0A7J7QTI3;
DT   07-APR-2021, integrated into UniProtKB/TrEMBL.
DT   07-APR-2021, sequence version 1.
DT   05-FEB-2025, entry version 16.
DE   RecName: Full=Tyrosine 3-monooxygenase {ECO:0000256|ARBA:ARBA00017181};
DE            EC=1.14.16.2 {ECO:0000256|ARBA:ARBA00011993};
DE   AltName: Full=Tyrosine 3-hydroxylase {ECO:0000256|ARBA:ARBA00032379};
GN   ORFNames=mMyoMyo1_019069 {ECO:0000313|EMBL:KAF6267146.1};
OS   Myotis myotis (Greater mouse-eared bat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Chiroptera; Yangochiroptera; Vespertilionidae;
OC   Myotis.
OX   NCBI_TaxID=51298 {ECO:0000313|EMBL:KAF6267146.1, ECO:0000313|Proteomes:UP000527355};
RN   [1] {ECO:0000313|EMBL:KAF6267146.1, ECO:0000313|Proteomes:UP000527355}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MMyoMyo1 {ECO:0000313|EMBL:KAF6267146.1};
RC   TISSUE=Flight muscle {ECO:0000313|EMBL:KAF6267146.1};
RX   PubMed=32699395;
RA   Jebb D., Huang Z., Pippel M., Hughes G.M., Lavrichenko K., Devanna P.,
RA   Winkler S., Jermiin L.S., Skirmuntt E.C., Katzourakis A., Burkitt-Gray L.,
RA   Ray D.A., Sullivan K.A.M., Roscito J.G., Kirilenko B.M., Davalos L.M.,
RA   Corthals A.P., Power M.L., Jones G., Ransome R.D., Dechmann D.K.N.,
RA   Locatelli A.G., Puechmaille S.J., Fedrigo O., Jarvis E.D., Hiller M.,
RA   Vernes S.C., Myers E.W., Teeling E.C.;
RT   "Six reference-quality genomes reveal evolution of bat adaptations.";
RL   Nature 583:578-584(2020).
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; Evidence={ECO:0000256|ARBA:ARBA00033689};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18202;
CC         Evidence={ECO:0000256|ARBA:ARBA00033689};
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000256|ARBA:ARBA00001954,
CC         ECO:0000256|PIRSR:PIRSR601273-2};
CC   -!- PATHWAY: Catecholamine biosynthesis; dopamine biosynthesis; dopamine
CC       from L-tyrosine: step 1/2. {ECO:0000256|ARBA:ARBA00004700}.
CC   -!- SUBCELLULAR LOCATION: Cell projection, axon
CC       {ECO:0000256|ARBA:ARBA00004489}. Cytoplasm, perinuclear region
CC       {ECO:0000256|ARBA:ARBA00004556}.
CC   -!- SIMILARITY: Belongs to the biopterin-dependent aromatic amino acid
CC       hydroxylase family. {ECO:0000256|ARBA:ARBA00009712}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KAF6267146.1}.
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DR   EMBL; JABWUV010000061; KAF6267146.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A7J7QTI3; -.
DR   VEuPathDB; HostDB:GeneID_118659614; -.
DR   UniPathway; UPA00747; UER00733.
DR   Proteomes; UP000527355; Unassembled WGS sequence.
DR   GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR   GO; GO:0043204; C:perikaryon; IEA:TreeGrafter.
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:0006585; P:dopamine biosynthetic process from tyrosine; IEA:TreeGrafter.
DR   GO; GO:0007507; P:heart development; IEA:TreeGrafter.
DR   GO; GO:0045471; P:response to ethanol; IEA:TreeGrafter.
DR   GO; GO:0001666; P:response to hypoxia; IEA:TreeGrafter.
DR   CDD; cd03345; eu_TyrOH; 1.
DR   FunFam; 1.10.800.10:FF:000002; Tyrosine 3-monooxygenase; 1.
DR   FunFam; 3.30.70.260:FF:000024; Tyrosine 3-monooxygenase; 1.
DR   Gene3D; 3.30.70.260; -; 1.
DR   Gene3D; 1.10.800.10; Aromatic amino acid hydroxylase; 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; IPR049321; TH_ACT.
DR   InterPro; IPR005962; Tyr_3_mOase.
DR   InterPro; IPR019773; Tyrosine_3-monooxygenase-like.
DR   InterPro; IPR021164; Tyrosine_hydroxylase_CS.
DR   NCBIfam; TIGR01269; Tyr_3_monoox; 1.
DR   PANTHER; PTHR11473; AROMATIC AMINO ACID HYDROXYLASE; 1.
DR   PANTHER; PTHR11473:SF18; TYROSINE 3-MONOOXYGENASE; 1.
DR   Pfam; PF00351; Biopterin_H; 1.
DR   Pfam; PF21417; TH_ACT; 1.
DR   Pfam; PF12549; TOH_N; 1.
DR   PIRSF; PIRSF000336; TH; 1.
DR   PRINTS; PR00372; FYWHYDRXLASE.
DR   SUPFAM; SSF55021; ACT-like; 1.
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   3: Inferred from homology;
KW   Catecholamine biosynthesis {ECO:0000256|ARBA:ARBA00022584};
KW   Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR000336-1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR000336-1};
KW   Monooxygenase {ECO:0000256|ARBA:ARBA00023033};
KW   Neurotransmitter biosynthesis {ECO:0000256|ARBA:ARBA00022979};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000527355}.
FT   DOMAIN          128..474
FT                   /note="Biopterin-dependent aromatic amino acid hydroxylase
FT                   family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS51410"
FT   REGION          25..47
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         307
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000336-1"
FT   BINDING         312
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000336-1"
FT   BINDING         352
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000336-1"
SQ   SEQUENCE   474 AA;  53357 MW;  A8959D58FB2E672C CRC64;
     MDSQPLLEEE SPRFIGRRQS LIEDARKERE KAEAAAAASE PGEPLGAGAC VERDGKALLN
     LLFTLRGAKT APLSRALKAF ETFEAQILHL ETRPAQRPRG GAPHLEYFVR CEVPSADLPH
     LLSSVRRVAE DVRGPGESRV LWFPRKVSEL DKCHHLVTKF DPDLDLDHPG FSDQEYRQRR
     RLIAEIAFQY RHGDPIPHVE YTAEEIATWK AVYTTLKGLY ATHACREHLE AFELLERFCG
     YQEDSIPQLE AVSRFLKERT GFQLRPVAGL LSARDFLASL AFRVFQCTQY IRHASSPMHS
     PEPDCCHELL GHVPMLADRT FAQFSQDIGL ASLGASDEEI EKLSTLYWFT VEFGLCKQNG
     EVKAYGAGLL SSYGELLHAL SEEPEIRAFD PDAAALQPYQ DQTYQSVYFV SESFSDAKDK
     LRSYAARIQR PFSVKFDPYT QAIDVLDSPR AIRSSLEGIQ DEMHALTHAL SAIS
//
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