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Database: UniProt
Entry: Q2ILP1_ANADE
LinkDB: Q2ILP1_ANADE
Original site: Q2ILP1_ANADE 
ID   Q2ILP1_ANADE            Unreviewed;       529 AA.
AC   Q2ILP1;
DT   07-MAR-2006, integrated into UniProtKB/TrEMBL.
DT   07-MAR-2006, sequence version 1.
DT   27-MAR-2024, entry version 93.
DE   SubName: Full=Phenylalanine 4-hydroxylase {ECO:0000313|EMBL:ABC82570.1};
DE            EC=1.14.16.1 {ECO:0000313|EMBL:ABC82570.1};
GN   OrderedLocusNames=Adeh_2800 {ECO:0000313|EMBL:ABC82570.1};
OS   Anaeromyxobacter dehalogenans (strain 2CP-C).
OC   Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC   Anaeromyxobacteraceae; Anaeromyxobacter.
OX   NCBI_TaxID=290397 {ECO:0000313|EMBL:ABC82570.1, ECO:0000313|Proteomes:UP000001935};
RN   [1] {ECO:0000313|EMBL:ABC82570.1, ECO:0000313|Proteomes:UP000001935}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2CP-C {ECO:0000313|EMBL:ABC82570.1,
RC   ECO:0000313|Proteomes:UP000001935};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C., Tapia R.,
RA   Gilna P., Kiss H., Schmutz J., Larimer F., Land M., Kyrpides N.,
RA   Anderson I., Sanford R.A., Ritalahti K.M., Thomas H.S., Kirby J.R.,
RA   Zhulin I.B., Loeffler F.E., Richardson P.;
RT   "Complete sequence of Anaeromyxobacter dehalogenans 2CP-C.";
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000001935}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2CP-C {ECO:0000313|Proteomes:UP000001935};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C., Tapia R.,
RA   Gilna P., Kiss H., Schmutz J., Larimer F., Land M., Kyrpides N.,
RA   Anderson I., Sanford R.A., Ritalahti K.M., Thomas H.S., Kirby J.R.,
RA   Zhulin I.B., Loeffler F.E., Richardson P.;
RT   "Complete sequence of Anaeromyxobacter dehalogenans 2CP-C.";
RL   Submitted (JAN-2006) 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}.
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DR   EMBL; CP000251; ABC82570.1; -; Genomic_DNA.
DR   RefSeq; WP_011421852.1; NC_007760.1.
DR   AlphaFoldDB; Q2ILP1; -.
DR   STRING; 290397.Adeh_2800; -.
DR   KEGG; ade:Adeh_2800; -.
DR   eggNOG; COG3186; Bacteria.
DR   HOGENOM; CLU_034458_0_0_7; -.
DR   OrthoDB; 9780502at2; -.
DR   Proteomes; UP000001935; Chromosome.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0004505; F:phenylalanine 4-monooxygenase activity; IEA:UniProtKB-EC.
DR   CDD; cd00361; arom_aa_hydroxylase; 1.
DR   Gene3D; 1.10.800.10; Aromatic amino acid hydroxylase; 1.
DR   InterPro; IPR001273; ArAA_hydroxylase.
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:SF24; PHENYLALANINE-4-HYDROXYLASE; 1.
DR   Pfam; PF00351; Biopterin_H; 2.
DR   SUPFAM; SSF56534; Aromatic aminoacid monoxygenases, catalytic and oligomerization domains; 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   ECO:0000313|EMBL:ABC82570.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001935}.
FT   DOMAIN          1..339
FT                   /note="Biopterin-dependent aromatic amino acid hydroxylase
FT                   family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS51410"
FT   BINDING         128
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601273-2"
FT   BINDING         133
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601273-2"
FT   BINDING         218
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601273-2"
SQ   SEQUENCE   529 AA;  57415 MW;  D4B23F173903DE88 CRC64;
     MGPTERAIAE LPPHLRRFVV AQDHAAYTPR DHAVWRHVLR RLTAHLATRA HPRYLAGLAA
     TGIEVERIPS LDEMNRKLAR VGWSAVAVRG FIPPAVFTEL QSRRVLAIAA DIRTHEHIEY
     TPAPDIIHES AGHAPFIADP TYAEYLRRAG EVGFRAIASA EDQAVFEAIR NLSVVKEDPE
     ASEEEVALSE ARLRAASASV RYASESTRAS RLYWWTAEYG LVGTLDDPRI YGAGLLSSIG
     EAVHCLTPAV RKLPLDPGCA DVAYDITRMQ PQLFVARDFD QLFEVLDAFD AGLSWRRGGD
     RGLEEARRAR TVNHLALSGG RELTGKVAER IPAATEIAPG LSTALVRLDG PVLVSRDGRA
     EGKPWPGEVV VAFGDAAVPE RGPFDLALPG GLALRGFAVG GGEVVDLRAT RDGRPLELPT
     WALLFVSRDL RSVAGGPADP GAWDRWFGEH GTFTAGEGEA RARARKAKAL PPALAALYDE
     VRRLRETGRA TRERLLAIRE AAAAFPGDWL LRAEVDELLA PGAEAGAHP
//
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