ID A0A1I8P648_STOCA Unreviewed; 573 AA.
AC A0A1I8P648;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=tryptophan 5-monooxygenase {ECO:0000256|ARBA:ARBA00012002};
DE EC=1.14.16.4 {ECO:0000256|ARBA:ARBA00012002};
GN Name=106092589 {ECO:0000313|EnsemblMetazoa:SCAU005130-PA};
OS Stomoxys calcitrans (Stable fly) (Conops calcitrans).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Muscoidea;
OC Muscidae; Stomoxys.
OX NCBI_TaxID=35570 {ECO:0000313|EnsemblMetazoa:SCAU005130-PA, ECO:0000313|Proteomes:UP000095300};
RN [1] {ECO:0000313|EnsemblMetazoa:SCAU005130-PA}
RP IDENTIFICATION.
RC STRAIN=USDA {ECO:0000313|EnsemblMetazoa:SCAU005130-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin + L-tryptophan + O2
CC = (4aS,6R)-4a-hydroxy-L-erythro-5,6,7,8-tetrahydrobiopterin + 5-
CC hydroxy-L-tryptophan; Xref=Rhea:RHEA:16709, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:15642, ChEBI:CHEBI:57912, ChEBI:CHEBI:58266,
CC ChEBI:CHEBI:59560; EC=1.14.16.4;
CC Evidence={ECO:0000256|ARBA:ARBA00001456};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000256|ARBA:ARBA00001954,
CC ECO:0000256|PIRSR:PIRSR601273-2};
CC -!- PATHWAY: Aromatic compound metabolism; serotonin biosynthesis;
CC serotonin from L-tryptophan: step 1/2. {ECO:0000256|ARBA:ARBA00004783}.
CC -!- SIMILARITY: Belongs to the biopterin-dependent aromatic amino acid
CC hydroxylase family. {ECO:0000256|ARBA:ARBA00009712}.
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DR RefSeq; XP_013114930.1; XM_013259476.1.
DR AlphaFoldDB; A0A1I8P648; -.
DR STRING; 35570.A0A1I8P648; -.
DR EnsemblMetazoa; SCAU005130-RA; SCAU005130-PA; SCAU005130.
DR GeneID; 106092589; -.
DR KEGG; scac:106092589; -.
DR VEuPathDB; VectorBase:SCAU005130; -.
DR OrthoDB; 275463at2759; -.
DR UniPathway; UPA00846; UER00799.
DR Proteomes; UP000095300; Unassembled WGS sequence.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0004510; F:tryptophan 5-monooxygenase activity; IEA:UniProtKB-EC.
DR GO; GO:0009072; P:aromatic amino acid metabolic process; IEA:InterPro.
DR GO; GO:0042427; P:serotonin biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd04929; ACT_TPH; 1.
DR CDD; cd03346; eu_TrpOH; 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; IPR005963; Trp_5_mOase.
DR InterPro; IPR041904; TrpOH_cat.
DR NCBIfam; TIGR01270; Trp_5_monoox; 1.
DR PANTHER; PTHR11473; AROMATIC AMINO ACID HYDROXYLASE; 1.
DR PANTHER; PTHR11473:SF40; TRYPTOPHAN 5-MONOOXYGENASE; 1.
DR Pfam; PF00351; Biopterin_H; 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 Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR601273-2};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR601273-2};
KW Monooxygenase {ECO:0000256|ARBA:ARBA00023033};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Serotonin biosynthesis {ECO:0000256|ARBA:ARBA00023094}.
FT DOMAIN 89..165
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT DOMAIN 171..518
FT /note="Biopterin-dependent aromatic amino acid hydroxylase
FT family profile"
FT /evidence="ECO:0000259|PROSITE:PS51410"
FT REGION 24..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 540..573
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 540..563
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 313
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000256|PIRSR:PIRSR601273-1"
FT BINDING 335
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000256|PIRSR:PIRSR601273-1"
FT BINDING 343
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000256|PIRSR:PIRSR601273-1"
FT BINDING 350
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|PIRSR:PIRSR601273-2"
FT BINDING 355
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|PIRSR:PIRSR601273-2"
FT BINDING 395
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|PIRSR:PIRSR601273-2"
FT BINDING 415
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000256|PIRSR:PIRSR601273-1"
FT BINDING 445
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000256|PIRSR:PIRSR601273-1"
SQ SEQUENCE 573 AA; 63887 MW; 9F17A3E284B6EC09 CRC64;
MSASGKSLLG LWLYRSGEQE WAVKQGSPLH GPRNKKDLGG SDSIENPGLN NVNNKLNSMT
SDMLGCGGGV GVGGAGAGQA PCSPGDRVSI IFTLKNQVGN LARALQVFQE LGINVLHLEL
SPLENATNQA DVVVDVECDP KRLDQVLQML NREVHSVNFT SVDKNALVRA PSLSACSSFD
FGDMMWFPRK IADLDKAQNV LMYGSELDAD HPGFKDPIYR KRREKFYSIA MNFKHGNPIP
RVQYTPEEIK TWGTVFNELH RLYIKYAVPE YMENWPELVK YCGYREDNIP QLQDVSTFLK
RKTGFQLRPV AGYLSPRDFL SGLAFRVFHC TQYIRHSSDP FYTPEPDCCH ELLGHMPLLA
NPSFAQFSQE IGLASLGASD ADIEKLATLY FFTVEFGLCH QSDNSFKVYG AGLLSSVAEL
QHALTCKEKI KKFDPEVTCK EECIITSYQN AYYYTESFEE AKEKMRSFAE SIQRPFGVRY
NPYTQSVEVL SNAQKITAVV SELKGDLSIV CSALRKISAT DETLDVESIA NMLQTSLNVR
GDRTPQNAIS PDNSDNSQHS IVVHTPDELG EMD
//
