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Database: UniProt
Entry: A0A2G5VDC9_9PELO
LinkDB: A0A2G5VDC9_9PELO
Original site: A0A2G5VDC9_9PELO 
ID   A0A2G5VDC9_9PELO        Unreviewed;       602 AA.
AC   A0A2G5VDC9;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   08-NOV-2023, entry version 12.
DE   RecName: Full=Biopterin-dependent aromatic amino acid hydroxylase family profile domain-containing protein {ECO:0000259|PROSITE:PS51410};
GN   Name=Cni-cat-2 {ECO:0000313|EMBL:PIC49774.1};
GN   Synonyms=Cnig_chr_II.g8271 {ECO:0000313|EMBL:PIC49774.1};
GN   ORFNames=B9Z55_008271 {ECO:0000313|EMBL:PIC49774.1};
OS   Caenorhabditis nigoni.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=1611254 {ECO:0000313|EMBL:PIC49774.1, ECO:0000313|Proteomes:UP000230233};
RN   [1] {ECO:0000313|Proteomes:UP000230233}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JU1422 {ECO:0000313|Proteomes:UP000230233};
RA   Yin D., Schwarz E.M., Thomas C.G., Felde R.L., Korf I.F., Cutter A.D.,
RA   Schartner C.M., Ralston E.J., Meyer B.J., Haag E.S.;
RT   "Rapid genome shrinkage in a self-fertile nematode reveals novel sperm
RT   competition proteins.";
RL   Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PIC49774.1}.
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DR   EMBL; PDUG01000002; PIC49774.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2G5VDC9; -.
DR   STRING; 1611254.A0A2G5VDC9; -.
DR   Proteomes; UP000230233; Chromosome ii.
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   PANTHER; PTHR11473; AROMATIC AMINO ACID HYDROXYLASE; 1.
DR   PANTHER; PTHR11473:SF15; TYROSINE 3-MONOOXYGENASE; 1.
DR   Pfam; PF00351; Biopterin_H; 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: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   Reference proteome {ECO:0000313|Proteomes:UP000230233}.
FT   DOMAIN          251..597
FT                   /note="Biopterin-dependent aromatic amino acid hydroxylase
FT                   family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS51410"
FT   BINDING         430
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601273-2"
FT   BINDING         435
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601273-2"
FT   BINDING         475
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601273-2"
SQ   SEQUENCE   602 AA;  68149 MW;  79E38E021318DC5A CRC64;
     MMIIGRKPMC SVYSRKEQQL SVSQDEDEEW EKEIFLGRWG GAITLFWIGY KFTTVTLTPL
     FQKLSSPLAK LIAAVNVARN VSINMSSLTN PTNTVMEEEE NPVAAPIQRG NKNPRRYSLV
     HQASCETQHH IGIRRQNTIQ HRKQLTDQMR GQKILQQLND EGVEVIFAAN DVSSIDFSVI
     VTSTDYISTF VSDILYNMKS AGVQICHVET RESKTVSGHD VLLDCRATKN QLIQAAELLT
     QNHVALTHFS IFSKKSVEKS QSMIWFPRHI SELDQCSKCI TKYEPTTDPR HPGHGDEEYI
     ARRKFLNDQA LEFKFGDEIG YVEYTEDEHA TWKAVYEKLG GLHESHTCGV YRQNLKILQK
     EKVLTADRIP QIRDVNKFLQ KKTGFELRPC SGLLSARDFL ASLAFRVFQT TTYLRHHKSP
     HHSPEPDLIH ELLGHVPMFS DPLLAQMSQD IGLMSLGASD EHIEKLATVY WFIVEFGLCK
     EDGKLKAIGA GLLSAYGELI HACSDAPEHK DFDPAVTAIQ KYEDDDYQPL YFVADSIHDA
     LAKLRKYASS MDRPFSVVYD PFTKSIETIQ SSADLEKAFS RLSNDLSAIT HAADRMKISI
     AA
//
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