Q03304 (TMOF_PSEME) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 70.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Toluene-4-monooxygenase electron transfer component Including the following 2 domains:
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| Gene names |
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| Organism | Pseudomonas mendocina | ||
| Taxonomic identifier | 300 [NCBI] | ||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas |
Protein attributes
| Sequence length | 326 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Electron transfer component of toluene 4-monooxygenase complex. |
| Catalytic activity | Reduced ferredoxin + NAD+ = oxidized ferredoxin + NADH. |
| Cofactor | FAD. Binds 1 2Fe-2S cluster per subunit By similarity. |
| Pathway | |
| Subunit structure | The multicomponent enzyme toluene-4-monooxygenase is formed by the tmoA, tmoB, tmoC, tmoD, tmoE and tmoF polypeptides. |
| Sequence similarities | Belongs to the bacterial ring-hydroxylating dioxygenase ferredoxin reductase family. Contains 1 2Fe-2S ferredoxin-type domain. Contains 1 FAD-binding FR-type domain. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Aromatic hydrocarbons catabolism |
| Ligand | 2Fe-2S FAD Flavoprotein Iron Iron-sulfur Metal-binding NAD |
| Molecular function | Oxidoreductase |
| Technical term | Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | aromatic compound catabolic process Inferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | 2 iron, 2 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW electron carrier activityInferred from electronic annotation. Source: InterPro ferredoxin-NAD+ reductase activityInferred from electronic annotation. Source: EC metal ion bindingInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 326 | 326 | Toluene-4-monooxygenase electron transfer component | PRO_0000167658 | |||||
Regions | |||||||||
| Domain | 1 – 92 | 92 | 2Fe-2S ferredoxin-type | ||||||
| Domain | 100 – 195 | 96 | FAD-binding FR-type | ||||||
| Region | 95 – 326 | 232 | Ferredoxin-reductase | ||||||
Sites | |||||||||
| Metal binding | 36 | 1 | Iron-sulfur (2Fe-2S) By similarity | ||||||
| Metal binding | 41 | 1 | Iron-sulfur (2Fe-2S) By similarity | ||||||
| Metal binding | 44 | 1 | Iron-sulfur (2Fe-2S) By similarity | ||||||
| Metal binding | 76 | 1 | Iron-sulfur (2Fe-2S) By similarity | ||||||
Sequences
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References
| [1] | "Identification of a new gene, tmoF, in the Pseudomonas mendocina KR1 gene cluster encoding toluene-4-monooxygenase." Yen K.-M., Karl M.R. J. Bacteriol. 174:7253-7261(1992) [PubMed: 1429451] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-14. Strain: KR1. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | M95045 Genomic DNA. Translation: AAA26004.1. |
| PIR | A47016. |
3D structure databases | |
| ProteinModelPortal | Q03304. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Family and domain databases | |
| InterPro | IPR006058. 2Fe2S_fd_BS. IPR012675. Beta-grasp_ferredoxin-type. IPR017927. Fd_Rdtase_FAD-bd. IPR001041. Ferredoxin. IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase. IPR008333. OxRdtase_FAD-bd_dom. IPR001433. OxRdtase_FAD/NAD-bd. IPR001221. Phe_hydroxylase. IPR017938. Riboflavin_synthase-like_b-brl. [Graphical view] |
| Gene3D | G3DSA:3.10.20.30. Ferredoxin_fold. 1 hit. |
| Pfam | PF00970. FAD_binding_6. 1 hit. PF00111. Fer2. 1 hit. PF00175. NAD_binding_1. 1 hit. [Graphical view] |
| PRINTS | PR00371. FPNCR. PR00410. PHEHYDRXLASE. |
| SUPFAM | SSF54292. Ferredoxin. 1 hit. SSF63380. Riboflavin_synthase_like_b-brl. 1 hit. |
| PROSITE | PS00197. 2FE2S_FER_1. 1 hit. PS51085. 2FE2S_FER_2. 1 hit. PS51384. FAD_FR. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | TMOF_PSEME | ||||||||
| Accession | Primary (citable) accession number: Q03304 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

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