ID A0A1I7SW20_BURXY Unreviewed; 549 AA.
AC A0A1I7SW20;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=BH4_AAA_HYDROXYL_2 domain-containing protein {ECO:0000313|WBParaSite:BXY_1725000.1};
OS Bursaphelenchus xylophilus (Pinewood nematode worm) (Aphelenchoides
OS xylophilus).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Tylenchomorpha; Aphelenchoidea; Aphelenchoididae;
OC Bursaphelenchus.
OX NCBI_TaxID=6326 {ECO:0000313|Proteomes:UP000095284, ECO:0000313|WBParaSite:BXY_1725000.1};
RN [1] {ECO:0000313|WBParaSite:BXY_1725000.1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (NOV-2016) 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 -!- SIMILARITY: Belongs to the biopterin-dependent aromatic amino acid
CC hydroxylase family. {ECO:0000256|ARBA:ARBA00009712}.
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DR AlphaFoldDB; A0A1I7SW20; -.
DR WBParaSite; BXY_1725000.1; BXY_1725000.1; BXY_1725000.
DR eggNOG; KOG3820; Eukaryota.
DR Proteomes; UP000095284; Unplaced.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0016714; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced pteridine as one donor, and incorporation of one atom of oxygen; IEA:InterPro.
DR GO; GO:0009072; P:aromatic amino acid metabolic process; IEA:InterPro.
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; IPR019773; Tyrosine_3-monooxygenase-like.
DR PANTHER; PTHR11473; AROMATIC AMINO ACID HYDROXYLASE; 1.
DR PANTHER; PTHR11473:SF40; TRYPTOPHAN 5-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 3: Inferred from homology;
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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 196..549
FT /note="Biopterin-dependent aromatic amino acid hydroxylase
FT family profile"
FT /evidence="ECO:0000259|PROSITE:PS51410"
FT BINDING 339
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000256|PIRSR:PIRSR601273-1"
FT BINDING 361
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000256|PIRSR:PIRSR601273-1"
FT BINDING 369
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000256|PIRSR:PIRSR601273-1"
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"
FT BINDING 446
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000256|PIRSR:PIRSR601273-1"
FT BINDING 476
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000256|PIRSR:PIRSR601273-1"
SQ SEQUENCE 549 AA; 63059 MW; 8EA78CE7F63CEE1A CRC64;
MRFPLRRFFG FVFKYRPTDS WPISEHCNSL FFILRSLEMA STMKFVYYNQ GIDQEVKNNN
ISDEKRLEDV KRRFRRSGSV GVPFVSEEEA KELKHQKTIE EVADENGILF LAMIITTKKT
SESISKILAL LPVEVSVKHI ESRDPKHGIH DDLEVFVEVE VPGHLPPDSV TAQLKAKGYV
VHEVSRTEIP LGAEEFRDPG SEDALSGCPW FPKAIKDLDI SGKRVIMYGA GGLDADHPGF
KDEEYRKRRM MFAEIALNYR QGDPIPRITY TDAEIKTWGV IYRRLRELHL KHACKEFLEN
FELLEKYCGY SENNIPQLED VSNFLKEKTG FRIRPVAGYL SARDFLAGLA FRVFNCTQYL
RHHADPFYTP EPDTVHELMG HMALFADPEF AQFSQELGLA SLGASEEDLK KLATLYFFSI
EFGLCTVDKK KPDEIGYKIY GAGLLSSAGE LVHAVEAQEK ILRFDPDRVV QQECLITTFQ
DNYFFTRSFD EVQQKLRTFT NSMNRPFVVR YNPYTESIEV LNNKRSIMLA VNSLRSDINL
LAGSLRNIL
//
