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Database: UniProt
Entry: Q1ISS1_KORVE
LinkDB: Q1ISS1_KORVE
Original site: Q1ISS1_KORVE 
ID   Q1ISS1_KORVE            Unreviewed;       250 AA.
AC   Q1ISS1;
DT   13-JUN-2006, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2006, sequence version 1.
DT   27-MAR-2024, entry version 78.
DE   SubName: Full=Phenylalanine 4-hydroxylase {ECO:0000313|EMBL:ABF40079.1};
DE            EC=1.14.16.1 {ECO:0000313|EMBL:ABF40079.1};
GN   OrderedLocusNames=Acid345_1076 {ECO:0000313|EMBL:ABF40079.1};
OS   Koribacter versatilis (strain Ellin345).
OC   Bacteria; Acidobacteriota; Terriglobia; Terriglobales; Acidobacteriaceae;
OC   Koribacter.
OX   NCBI_TaxID=204669 {ECO:0000313|EMBL:ABF40079.1, ECO:0000313|Proteomes:UP000002432};
RN   [1] {ECO:0000313|EMBL:ABF40079.1, ECO:0000313|Proteomes:UP000002432}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ellin345 {ECO:0000313|EMBL:ABF40079.1,
RC   ECO:0000313|Proteomes:UP000002432};
RX   PubMed=19201974; DOI=10.1128/AEM.02294-08;
RA   Ward N.L., Challacombe J.F., Janssen P.H., Henrissat B., Coutinho P.M.,
RA   Wu M., Xie G., Haft D.H., Sait M., Badger J., Barabote R.D., Bradley B.,
RA   Brettin T.S., Brinkac L.M., Bruce D., Creasy T., Daugherty S.C.,
RA   Davidsen T.M., DeBoy R.T., Detter J.C., Dodson R.J., Durkin A.S.,
RA   Ganapathy A., Gwinn-Giglio M., Han C.S., Khouri H., Kiss H., Kothari S.P.,
RA   Madupu R., Nelson K.E., Nelson W.C., Paulsen I., Penn K., Ren Q.,
RA   Rosovitz M.J., Selengut J.D., Shrivastava S., Sullivan S.A., Tapia R.,
RA   Thompson L.S., Watkins K.L., Yang Q., Yu C., Zafar N., Zhou L., Kuske C.R.;
RT   "Three genomes from the phylum Acidobacteria provide insight into the
RT   lifestyles of these microorganisms in soils.";
RL   Appl. Environ. Microbiol. 75:2046-2056(2009).
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; CP000360; ABF40079.1; -; Genomic_DNA.
DR   RefSeq; WP_011521881.1; NC_008009.1.
DR   AlphaFoldDB; Q1ISS1; -.
DR   STRING; 204669.Acid345_1076; -.
DR   EnsemblBacteria; ABF40079; ABF40079; Acid345_1076.
DR   KEGG; aba:Acid345_1076; -.
DR   eggNOG; COG3186; Bacteria.
DR   HOGENOM; CLU_023198_1_0_0; -.
DR   OrthoDB; 9780502at2; -.
DR   Proteomes; UP000002432; 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; 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:SF24; PHENYLALANINE-4-HYDROXYLASE; 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   ECO:0000313|EMBL:ABF40079.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002432}.
FT   DOMAIN          1..250
FT                   /note="Biopterin-dependent aromatic amino acid hydroxylase
FT                   family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS51410"
FT   BINDING         126
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601273-2"
FT   BINDING         131
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601273-2"
FT   BINDING         172
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601273-2"
SQ   SEQUENCE   250 AA;  28836 MW;  5793ABEFD3CBD41B CRC64;
     MQPHTMTLPG DAAEYVVTQH YDQYSDVEHG TWKTLYERRM EQLSTHACKE YLEGLRVLGM
     RAERMPVISD INKTLQTRTN WMLLPVSGFL PGRTFFDLLA ARVFPVTTYI RKPDSLDYTP
     EPDIFHDIFG HVPMHAHKVF ADYLQAFAQI ARQITNDADQ ERLGRLFWYT VEFGLIREGS
     DVKMYGSGVI SSVKEGDNVV HRGCKIHDFS LEEVLDTHVK VDELQPTLFA IENFEQIYEA
     TKEARKVFGV
//
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