ID A0A3Q2V8P4_HAPBU Unreviewed; 461 AA.
AC A0A3Q2V8P4;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=phenylalanine 4-monooxygenase {ECO:0000256|ARBA:ARBA00011995};
DE EC=1.14.16.1 {ECO:0000256|ARBA:ARBA00011995};
DE AltName: Full=Phe-4-monooxygenase {ECO:0000256|ARBA:ARBA00029922};
OS Haplochromis burtoni (Burton's mouthbrooder) (Chromis burtoni).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Haplochromis.
OX NCBI_TaxID=8153 {ECO:0000313|Ensembl:ENSHBUP00000007010.1, ECO:0000313|Proteomes:UP000264840};
RN [1] {ECO:0000313|Ensembl:ENSHBUP00000007010.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin + L-phenylalanine +
CC O2 = (4aS,6R)-4a-hydroxy-L-erythro-5,6,7,8-tetrahydrobiopterin + L-
CC tyrosine; Xref=Rhea:RHEA:20273, ChEBI:CHEBI:15379, ChEBI:CHEBI:15642,
CC ChEBI:CHEBI:58095, ChEBI:CHEBI:58315, ChEBI:CHEBI:59560;
CC EC=1.14.16.1; Evidence={ECO:0000256|ARBA:ARBA00001060};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000256|ARBA:ARBA00001954,
CC ECO:0000256|PIRSR:PIRSR601273-2};
CC -!- PATHWAY: Amino-acid degradation; L-phenylalanine degradation;
CC acetoacetate and fumarate from L-phenylalanine: step 1/6.
CC {ECO:0000256|ARBA:ARBA00005088}.
CC -!- SIMILARITY: Belongs to the biopterin-dependent aromatic amino acid
CC hydroxylase family. {ECO:0000256|ARBA:ARBA00009712}.
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DR RefSeq; XP_005934294.1; XM_005934232.1.
DR AlphaFoldDB; A0A3Q2V8P4; -.
DR STRING; 8153.ENSHBUP00000007010; -.
DR Ensembl; ENSHBUT00000004362.1; ENSHBUP00000007010.1; ENSHBUG00000008494.1.
DR GeneID; 102289427; -.
DR CTD; 5053; -.
DR GeneTree; ENSGT00950000182885; -.
DR OMA; FHDEVYR; -.
DR OrthoDB; 275463at2759; -.
DR UniPathway; UPA00139; UER00337.
DR Proteomes; UP000264840; Unplaced.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0004505; F:phenylalanine 4-monooxygenase activity; IEA:UniProtKB-EC.
DR GO; GO:0006559; P:L-phenylalanine catabolic process; IEA:UniProtKB-UniPathway.
DR CDD; cd03347; eu_PheOH; 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; IPR041912; Euk_PheOH_cat.
DR InterPro; IPR005961; Phe-4-hydroxylase_tetra.
DR InterPro; IPR019773; Tyrosine_3-monooxygenase-like.
DR NCBIfam; TIGR01268; Phe4hydrox_tetr; 1.
DR PANTHER; PTHR11473; AROMATIC AMINO ACID HYDROXYLASE; 1.
DR PANTHER; PTHR11473:SF24; PHENYLALANINE-4-HYDROXYLASE; 1.
DR Pfam; PF01842; ACT; 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 Reference proteome {ECO:0000313|Proteomes:UP000264840}.
FT DOMAIN 45..123
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT DOMAIN 115..461
FT /note="Biopterin-dependent aromatic amino acid hydroxylase
FT family profile"
FT /evidence="ECO:0000259|PROSITE:PS51410"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 294
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|PIRSR:PIRSR000336-1"
FT BINDING 299
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|PIRSR:PIRSR000336-1"
FT BINDING 339
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|PIRSR:PIRSR000336-1"
SQ SEQUENCE 461 AA; 52645 MW; D31FF0965EFD107C CRC64;
MDAAYKRVNG NYSPEAETGD QVPGQKRRGS MYLEEETNNK SEVISCIFSL KEEVGALAKA
LRLFEEKGIN LTHIESRPSR MNNEQYEFFI SVDSSCSQAL DEVIDCLRTQ ISGHVHELTR
SKEKDTVPWF PNDIQDLDRF ANQILSYGSE LDADHPGFTD PVYRARRKEF ADIAYNYRHG
QSIPRVEYTE EEKATWGTVF RELKTLYPTH ACREHNRVFP LLEKYCGYRP DNIPQLEDVS
RFLQSCTGFR LRPVAGLLSS RDFLAGLAFR VFHSTQYIRH GSKPTYTPEP DICHELLGHV
PLFADPSFAQ FSQEIGLASL GAPDEYIEKL ATVYWFTVEF GLCKQGSEIK AYGAGLLSSF
GELGYSLTEK PKLLPFDPEK TSVQKYPITE YQPVYFVAES FEDAKEKVRK FAGKIPKPFS
VRYNPYTQSI EVLDNTQQLR NLADSINSEM GKLCEALRKL E
//
