Reviewed,
UniProtKB/Swiss-Prot Q8XU39 (PH4H_RALSO)
Last modified
February 9, 2010.
Version 59.
History...
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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents
Names and origin
| Protein names | Recommended name: Phenylalanine-4-hydroxylase Short name=PAH EC=1.14.16.1 Alternative name(s): Phe-4-monooxygenase | ||||||
| Gene names |
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| Organism | Ralstonia solanacearum (Pseudomonas solanacearum) [Complete proteome] [HAMAP] | ||||||
| Taxonomic identifier | 305 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Ralstonia |
Protein attributes
| Sequence length | 313 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Catalytic activity | L-phenylalanine + tetrahydrobiopterin + O2 = L-tyrosine + 4a-hydroxytetrahydrobiopterin. |
| Cofactor | Binds 1 Fe2+ ion By similarity. |
| Pathway | |
| Sequence similarities | Belongs to the biopterin-dependent aromatic amino acid hydroxylase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Phenylalanine catabolism |
| Ligand | Iron Metal-binding |
| Molecular function | Monooxygenase Oxidoreductase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | L-phenylalanine catabolic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reductionInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW phenylalanine 4-monooxygenase activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
Sequences
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References
| [1] | "Genome sequence of the plant pathogen Ralstonia solanacearum." Salanoubat M., Genin S., Artiguenave F., Gouzy J., Mangenot S., Arlat M., Billault A., Brottier P., Camus J.-C., Cattolico L., Chandler M., Choisne N., Claudel-Renard C., Cunnac S., Demange N., Gaspin C., Lavie M., Moisan A. Boucher C.A.Nature 415:497-502(2002) [PubMed: 11823852] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: GMI1000. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AL646052 Genomic DNA. Translation: CAD17143.1. |
| RefSeq | NP_521474.1. |
3D structure databases | |
| SMR | Q8XU39. Positions 15-271, 42-301. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 1222219. |
| GenomeReviews | Gene locus RSc3355 in contig AL646052_GR. |
| KEGG | rso:RSc3355. |
| NMPDR | fig|267608.1.peg.3353. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | HBG403840. |
| OMA | FLARLYW. |
Enzyme and pathway databases | |
| BioCyc | RSOL267608:RSC3355-MONOMER. |
| BRENDA | 1.14.16.1. 97066. |
Family and domain databases | |
| InterPro | IPR001273. ArAA_hydroxylase. IPR018301. ArAA_hydroxylase_Fe/CU_BS. IPR019774. Aromatic-AA_hydroxylase_C. IPR005960. Phe-4-hydroxylase_mono. [Graphical view] |
| Gene3D | G3DSA:1.10.800.10. Aaa_hydroxylase. 1 hit. |
| PANTHER | PTHR11473. Aaa_hydroxylase. 1 hit. |
| Pfam | PF00351. Biopterin_H. 1 hit. [Graphical view] |
| PRINTS | PR00372. FYWHYDRXLASE. |
| TIGRFAMs | TIGR01267. Phe4hydrox_mono. 1 hit. |
| PROSITE | PS00367. BIOPTERIN_HYDROXYL. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | PH4H_RALSO | ||||||||
| Accession | Primary (citable) accession number: Q8XU39 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

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