ID A0A2D0QT84_ICTPU Unreviewed; 547 AA.
AC A0A2D0QT84;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Tryptophan 5-hydroxylase 2 {ECO:0000256|ARBA:ARBA00040889};
DE EC=1.14.16.4 {ECO:0000256|ARBA:ARBA00012002};
DE AltName: Full=Tryptophan 5-monooxygenase 2 {ECO:0000256|ARBA:ARBA00042662};
GN Name=tph2 {ECO:0000313|RefSeq:XP_017320700.1};
OS Ictalurus punctatus (Channel catfish) (Silurus punctatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC Ictaluridae; Ictalurus.
OX NCBI_TaxID=7998 {ECO:0000313|RefSeq:XP_017320700.1};
RN [1] {ECO:0000313|RefSeq:XP_017320700.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_017320700.1};
RG RefSeq;
RL Submitted (NOV-2023) 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_017320700.1; XM_017465211.3.
DR AlphaFoldDB; A0A2D0QT84; -.
DR STRING; 7998.ENSIPUP00000028089; -.
DR Ensembl; ENSIPUT00000029231; ENSIPUP00000028089; ENSIPUG00000019013.
DR GeneID; 108263971; -.
DR CTD; 121278; -.
DR OMA; VHFNPYT; -.
DR OrthoDB; 275463at2759; -.
DR UniPathway; UPA00846; UER00799.
DR Proteomes; UP000221080; Chromosome 4.
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 InterPro; IPR019773; Tyrosine_3-monooxygenase-like.
DR NCBIfam; TIGR01270; Trp_5_monoox; 1.
DR PANTHER; PTHR11473; AROMATIC AMINO ACID HYDROXYLASE; 1.
DR PANTHER; PTHR11473:SF16; TRYPTOPHAN 5-HYDROXYLASE 2; 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 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};
KW Serotonin biosynthesis {ECO:0000256|ARBA:ARBA00023094}.
FT BINDING 338
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000256|PIRSR:PIRSR601273-1"
FT BINDING 360
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000256|PIRSR:PIRSR601273-1"
FT BINDING 368
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000256|PIRSR:PIRSR601273-1"
FT BINDING 375
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|PIRSR:PIRSR000336-1"
FT BINDING 380
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|PIRSR:PIRSR000336-1"
FT BINDING 420
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|PIRSR:PIRSR000336-1"
FT BINDING 439
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000256|PIRSR:PIRSR601273-1"
FT BINDING 469
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000256|PIRSR:PIRSR601273-1"
SQ SEQUENCE 547 AA; 62510 MW; 9C4DFEA80664F650 CRC64;
MASQVQKKKG SEAVSVHSEV QGKTKPQETM SPLSDNHSQK KGSEIPKSPV GLLRKRGKEA
IPKMQPSMMM FSSKYWARRG LSLDSAMLDQ QHLGNNMLRR TSFSRIDEKE DSGSASDSSK
TAVIFSLKNE VGCLVKALRL FQEKHVNLAH IESRKSKRVT TEVEIYAECN CTKKEFNELV
QHLKDHVNII SYNTPENVWS VETDVEGVPW FPQKISELDQ CSHRVLMYGS ELDADHPGFK
DTIYRQRRKY FVEVAMNYKF GQPIPRIEYT REEVKTWGVV FRELTKLYPT HACREYIKNL
PLLTKHCGYR EDNIPQLEDV SLFLRERSGF TVRPVAGYLS PRDFLAGLAY RVFNCTQYVR
HSTDPLYTPE PDTCHELLGH VPLLADPKFA QFSQEIGLAS LGASDEDVQK LATCYFFTIE
FGLCKQDGQL RAYGAGLLSS IGELRHALSE KAVVKQFDPK TTCHQECLIT TFQDVYFVSE
SFEEAKERMR EFAKTIKRPF SVYYNPYTSS IDLLKDTRSI ENVVQDLRSD LTTVCDALGK
MNKYLGI
//
