ID E0VXJ5_PEDHC Unreviewed; 547 AA.
AC E0VXJ5;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 72.
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 Name=8236361 {ECO:0000313|EnsemblMetazoa:PHUM501080-PA};
GN ORFNames=Phum_PHUM501080 {ECO:0000313|EMBL:EEB18101.1};
OS Pediculus humanus subsp. corporis (Body louse).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Paraneoptera; Psocodea; Phthiraptera; Anoplura; Pediculidae;
OC Pediculus.
OX NCBI_TaxID=121224;
RN [1] {ECO:0000313|EMBL:EEB18101.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=USDA {ECO:0000313|EMBL:EEB18101.1};
RA Kirkness E., Hannick L., Hass B., Bruggner R., Lawson D., Bidwell S.,
RA Joardar V., Caler E., Walenz B., Inman J., Schobel S., Galinsky K.,
RA Amedeo P., Strausberg R.;
RT "Annotation of Pediculus humanus corporis strain USDA.";
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EEB18101.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=USDA {ECO:0000313|EMBL:EEB18101.1};
RG The Human Body Louse Genome Consortium;
RA Kirkness E., Walenz B., Hass B., Bruggner R., Strausberg R.;
RT "The genome of the human body louse.";
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblMetazoa:PHUM501080-PA}
RP IDENTIFICATION.
RC STRAIN=USDA {ECO:0000313|EnsemblMetazoa:PHUM501080-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
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}.
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DR EMBL; AAZO01006076; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DS235832; EEB18101.1; -; Genomic_DNA.
DR RefSeq; XP_002430839.1; XM_002430794.1.
DR AlphaFoldDB; E0VXJ5; -.
DR STRING; 121224.E0VXJ5; -.
DR EnsemblMetazoa; PHUM501080-RA; PHUM501080-PA; PHUM501080.
DR GeneID; 8236361; -.
DR KEGG; phu:Phum_PHUM501080; -.
DR CTD; 8236361; -.
DR VEuPathDB; VectorBase:PHUM501080; -.
DR eggNOG; KOG3820; Eukaryota.
DR HOGENOM; CLU_023198_0_1_1; -.
DR InParanoid; E0VXJ5; -.
DR OMA; VRYNPHT; -.
DR OrthoDB; 275463at2759; -.
DR UniPathway; UPA00747; UER00733.
DR Proteomes; UP000009046; Unassembled WGS sequence.
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 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; IPR045865; ACT-like_dom_sf.
DR InterPro; IPR002912; ACT_dom.
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; SSF55021; ACT-like; 1.
DR SUPFAM; SSF56534; Aromatic aminoacid monoxygenases, catalytic and oligomerization domains; 1.
DR PROSITE; PS51671; ACT; 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, ECO:0000313|EMBL:EEB18101.1};
KW Neurotransmitter biosynthesis {ECO:0000256|ARBA:ARBA00022979};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:EEB18101.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000009046}.
FT DOMAIN 127..202
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT DOMAIN 197..543
FT /note="Biopterin-dependent aromatic amino acid hydroxylase
FT family profile"
FT /evidence="ECO:0000259|PROSITE:PS51410"
FT BINDING 376
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|PIRSR:PIRSR000336-1"
FT BINDING 381
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|PIRSR:PIRSR000336-1"
FT BINDING 421
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|PIRSR:PIRSR000336-1"
SQ SEQUENCE 547 AA; 62472 MW; 1C51F5B9E75EF53F CRC64;
MSVATAQKNR EMFAVNKSYS VENGYPARRR SLVDDARFEA VVVKQNKQAG LEEARQKTNG
MFPSFISQQP NKRIPKFFVK IQKIFKMLNK FNFNQPPVDS ELTEEEMFIL NASSDSKIDD
KTIQRSTLML KLKDGIGSLA RILKTIENFK GTVVHVESRP SNVSGVQYDV LIKVDLTRQS
LLLLIRSLRQ SSALGGVSLL TDEKVNVKDP WFPRHARDLD NCNHLMTKYE PDLDMNHPGF
ADKVYRERRK IIADIAFAYK YGDPIPRIEY TESETSTWTA VFHTVKDLMP KHACQEYRKV
FAMLEEDGIF EANKIPQLED MSAFLKKHTG FTLRPAAGLL SARDFLASLA FRVFQSTQYV
RHTSSPYHTP EPDCIHELLG HMPLLADPSF AQFSQEIGLA SLGASDEEIE KLSTVYWFTV
EFGLCKEAGT VKAYGAGLLS SYGELLHAIS DKPEHRSFDP ASTAVQPYQD QEYQPIYYVA
ESFEDAKEKF RRWVSQMSRP FEVRFNPHTE RIEILDSVDK LEGLMSQLQL EMLHLTNAVN
KMRTTIC
//
