Reviewed,
UniProtKB/Swiss-Prot P43334 (PH4H_PSEAE)
Last modified
November 25, 2008.
Version 66.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
Customize display | text xml rdf/xml gff fasta |
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 |
| ||||
| Organism | Pseudomonas aeruginosa [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 287 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas |
Protein attributes
| Sequence length | 262 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Catalytic activity | L-phenylalanine + tetrahydrobiopterin + O(2) = L-tyrosine + 4a-hydroxytetrahydrobiopterin. |
| Cofactor | Binds 1 Fe(2+) ion. |
| Pathway | |
| Subunit structure | Monomer. |
| 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: InterPro oxidation reductionInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | iron ion binding Inferred from electronic annotation. Source: InterPro phenylalanine 4-monooxygenase activityInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 262 | 262 | Phenylalanine-4-hydroxylase | PRO_0000205555 | |||||
Sites | |||||||||
| Metal binding | 121 | 1 | Iron By similarity | ||||||
| Metal binding | 126 | 1 | Iron By similarity | ||||||
| Metal binding | 166 | 1 | Iron Potential | ||||||
Experimental info | |||||||||
| Sequence conflict | 135 | 1 | F → L in AAA25936. Ref.1 | ||||||
Sequences
| ||||||||||||||||||
References
| « Hide 'large scale' references | |
| [1] | "Pseudomonas aeruginosa possesses homologues of mammalian phenylalanine hydroxylase and 4 alpha-carbinolamine dehydratase/DCoH as part of a three-component gene cluster." Zhao G., Xia T., Song J., Roy R.A. Proc. Natl. Acad. Sci. U.S.A. 91:1366-1370(1994) [PubMed: 8108417] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228. |
| [2] | "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic pathogen." Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P., Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M., Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y., Brody L.L., Coulter S.N., Folger K.R. Olson M.V.Nature 406:959-964(2000) [PubMed: 10984043] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228. |
Cross-references
Sequence databases | |
|---|---|
| M88627 Genomic DNA. Translation: AAA25936.1. AE004091 Genomic DNA. Translation: AAG04261.1. | |
| PIR | A53452. F83535. |
| RefSeq | NP_249563.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1LTZ based on UniProtKB P30967. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 879709. |
| GenomeReviews | Gene locus PA0872 in contig AE004091_GR. |
| KEGG | pae:PA0872. |
Organism-specific databases | |
| PseudoCAP | PA0872. |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | P43334. |
Enzyme and pathway databases | |
| BioCyc | PAER208964:PA0872-MON. |
Family and domain databases | |
| InterPro | IPR001273. Aaa_hydroxylase. 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. |
| ProDom | PD002559. Aaa_hydroxylase. 1 hit. [Graphical view] [Entries sharing at least one domain] |
| TIGRFAMs | TIGR01267. Phe4hydrox_mono. 1 hit. |
| PROSITE | PS00367. BIOPTERIN_HYDROXYL. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | PH4H_PSEAE | ||||||||
| Accession | Primary (citable) accession number: P43334 | ||||||||
| Entry history |
| ||||||||
| 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 |

Clusters with


