(data stored in ACNUC7421 zone)

SWISSPROT: B4SR36_STRM5

ID   B4SR36_STRM5            Unreviewed;       297 AA.
AC   B4SR36;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   08-MAY-2019, entry version 54.
DE   SubName: Full=Phenylalanine-4-hydroxylase {ECO:0000313|EMBL:ACF49737.1};
DE            EC=1.14.16.1 {ECO:0000313|EMBL:ACF49737.1};
GN   OrderedLocusNames=Smal_0032 {ECO:0000313|EMBL:ACF49737.1};
OS   Stenotrophomonas maltophilia (strain R551-3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Stenotrophomonas;
OC   Stenotrophomonas maltophilia group.
OX   NCBI_TaxID=391008 {ECO:0000313|EMBL:ACF49737.1, ECO:0000313|Proteomes:UP000001867};
RN   [1] {ECO:0000313|EMBL:ACF49737.1, ECO:0000313|Proteomes:UP000001867}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R551-3 {ECO:0000313|EMBL:ACF49737.1,
RC   ECO:0000313|Proteomes:UP000001867};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L.,
RA   Lang D., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Taghavi S., Monchy S., Newman L., Vangronsveld J.,
RA   van der Lelie D., Richardson P.;
RT   "Complete sequence of Stenotrophomonas maltophilia R551-3.";
RL   Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP001111; ACF49737.1; -; Genomic_DNA.
DR   RefSeq; WP_012509617.1; NC_011071.1.
DR   STRING; 391008.Smal_0032; -.
DR   EnsemblBacteria; ACF49737; ACF49737; Smal_0032.
DR   KEGG; smt:Smal_0032; -.
DR   eggNOG; ENOG4105MIR; Bacteria.
DR   eggNOG; COG3186; LUCA.
DR   HOGENOM; HOG000253806; -.
DR   KO; K00500; -.
DR   OMA; KQFPVAT; -.
DR   OrthoDB; 1492162at2; -.
DR   BioCyc; SMAL391008:SMAL_RS00160-MONOMER; -.
DR   Proteomes; UP000001867; Chromosome.
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:InterPro.
DR   CDD; cd03348; pro_PheOH; 1.
DR   Gene3D; 1.10.800.10; -; 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   InterPro; IPR005960; Phe-4-hydroxylase_mono.
DR   PANTHER; PTHR11473; PTHR11473; 1.
DR   Pfam; PF00351; Biopterin_H; 1.
DR   PRINTS; PR00372; FYWHYDRXLASE.
DR   SUPFAM; SSF56534; SSF56534; 1.
DR   TIGRFAMs; TIGR01267; Phe4hydrox_mono; 1.
DR   PROSITE; PS00367; BH4_AAA_HYDROXYL_1; 1.
DR   PROSITE; PS51410; BH4_AAA_HYDROXYL_2; 1.
PE   4: Predicted;
DR   PRODOM; B4SR36.
DR   SWISS-2DPAGE; B4SR36.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001867};
KW   Oxidoreductase {ECO:0000313|EMBL:ACF49737.1}.
FT   DOMAIN        1    297       BH4_AAA_HYDROXYL_2. {ECO:0000259|PROSITE:
FT                                PS51410}.
SQ   SEQUENCE   297 AA;  33680 MW;  57E0E8D8CD41D16F CRC64;
     MDLAQPRRVE HQQTDKGYVP VYTTALVEQP WDTYTADDHA TWSTLYQRQR ELLVGRACQE
     FLDAQDEMGM SAHMIPRFDQ LNEVLGAATG WTLVGVEGLL PELDFFDHLA NRRFPVTWWI
     RRPDQIDYIA EPDLFHDLFG HVPLLMNPVF ANYMEAYGRG GVKAHAIGPD ALQNLTRLYW
     YTVEFGLIDT PDGLRIYGAG IVSSKGESLY SLESAAPNRI GFDLQRIMRT KYRIDTFQKT
     YFVIDSFEQL MQATSPDFTP IYAALSDQAH LPAGEVQADD RVFQKGTGEG WADGGDV
//

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