Reviewed,
UniProtKB/Swiss-Prot Q98D72 (PH4H_RHILO)
Last modified
February 9, 2010.
Version 55.
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 | Rhizobium loti (Mesorhizobium loti) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 381 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Phyllobacteriaceae › Mesorhizobium |
Protein attributes
| Sequence length | 275 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] | "Complete genome structure of the nitrogen-fixing symbiotic bacterium Mesorhizobium loti." Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S., Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Mochizuki Y., Nakayama S. Tabata S.DNA Res. 7:331-338(2000) [PubMed: 11214968] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: MAFF303099. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | BA000012 Genomic DNA. Translation: BAB51399.1. |
| RefSeq | NP_105613.1. |
3D structure databases | |
| SMR | Q98D72. Positions 23-275. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 1228274. |
| GenomeReviews | Gene locus mlr4831 in contig BA000012_GR. |
| KEGG | mlo:mlr4831. |
| NMPDR | fig|266835.1.peg.3717. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | HBG403840. |
| OMA | YKIDSYQ. |
Enzyme and pathway databases | |
| BRENDA | 1.14.16.1. 3315. |
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_RHILO | ||||||||
| Accession | Primary (citable) accession number: Q98D72 | ||||||||
| 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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