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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//