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Protein

Toluene-4-monooxygenase electron transfer component

Gene

tmoF

Organism
Pseudomonas mendocina
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Electron transfer component of toluene 4-monooxygenase complex.

Catalytic activityi

Reduced ferredoxin + NAD+ = oxidized ferredoxin + NADH.

Cofactori

Protein has several cofactor binding sites:

Pathwayi: toluene degradation

This protein is involved in the pathway toluene degradation, which is part of Xenobiotic degradation.
View all proteins of this organism that are known to be involved in the pathway toluene degradation and in Xenobiotic degradation.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi36 – 361Iron-sulfur (2Fe-2S)PROSITE-ProRule annotation
Metal bindingi41 – 411Iron-sulfur (2Fe-2S)PROSITE-ProRule annotation
Metal bindingi44 – 441Iron-sulfur (2Fe-2S)PROSITE-ProRule annotation
Metal bindingi76 – 761Iron-sulfur (2Fe-2S)PROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Aromatic hydrocarbons catabolism

Keywords - Ligandi

2Fe-2S, FAD, Flavoprotein, Iron, Iron-sulfur, Metal-binding, NAD

Enzyme and pathway databases

UniPathwayiUPA00273.

Names & Taxonomyi

Protein namesi
Recommended name:
Toluene-4-monooxygenase electron transfer component
Including the following 2 domains:
Ferredoxin
Ferredoxin--NAD(+) reductase (EC:1.18.1.3)
Gene namesi
Name:tmoF
OrganismiPseudomonas mendocina
Taxonomic identifieri300 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 326326Toluene-4-monooxygenase electron transfer componentPRO_0000167658Add
BLAST

Interactioni

Subunit structurei

The multicomponent enzyme toluene-4-monooxygenase is formed by the TmoA, TmoB, TmoC, TmoD, TmoE and TmoF polypeptides. The heterohexamer formed by two molecules each of TmoA, TmoB and TmoE interacts with the effector protein TmoD, the Rieske iron-sulfur protein TmoC and the NADH-containing oxidoreductase TmoF.

Structurei

Secondary structure

1
326
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 54Combined sources
Beta strandi9 – 113Combined sources
Beta strandi13 – 153Combined sources
Helixi21 – 277Combined sources
Beta strandi37 – 415Combined sources
Beta strandi45 – 517Combined sources
Beta strandi53 – 564Combined sources
Helixi65 – 695Combined sources
Beta strandi72 – 743Combined sources
Helixi75 – 773Combined sources
Beta strandi78 – 825Combined sources
Beta strandi84 – 885Combined sources
Beta strandi101 – 12323Combined sources
Beta strandi135 – 1406Combined sources
Turni141 – 1433Combined sources
Beta strandi144 – 1496Combined sources
Beta strandi158 – 1647Combined sources
Helixi170 – 1778Combined sources
Beta strandi181 – 1899Combined sources
Beta strandi202 – 2076Combined sources
Helixi208 – 2103Combined sources
Helixi211 – 22313Combined sources
Beta strandi230 – 2378Combined sources
Helixi239 – 24810Combined sources
Beta strandi255 – 2617Combined sources
Helixi277 – 2804Combined sources
Helixi281 – 2888Combined sources
Beta strandi292 – 2976Combined sources
Helixi299 – 31012Combined sources
Helixi317 – 3193Combined sources
Beta strandi320 – 3245Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4WQMX-ray1.62A2-326[»]
ProteinModelPortaliQ03304.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 92922Fe-2S ferredoxin-typePROSITE-ProRule annotationAdd
BLAST
Domaini100 – 19596FAD-binding FR-typePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni95 – 326232Ferredoxin-reductaseAdd
BLAST

Sequence similaritiesi

Contains 1 2Fe-2S ferredoxin-type domain.PROSITE-ProRule annotation
Contains 1 FAD-binding FR-type domain.PROSITE-ProRule annotation

Family and domain databases

CDDicd00207. fer2. 1 hit.
Gene3Di3.10.20.30. 1 hit.
InterProiIPR001041. 2Fe-2S_ferredoxin-type.
IPR006058. 2Fe2S_fd_BS.
IPR012675. Beta-grasp_dom.
IPR017927. Fd_Rdtase_FAD-bd.
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]
PfamiPF00970. FAD_binding_6. 1 hit.
PF00111. Fer2. 1 hit.
PF00175. NAD_binding_1. 1 hit.
[Graphical view]
PRINTSiPR00371. FPNCR.
PR00410. PHEHYDRXLASE.
SUPFAMiSSF54292. SSF54292. 1 hit.
SSF63380. SSF63380. 1 hit.
PROSITEiPS00197. 2FE2S_FER_1. 1 hit.
PS51085. 2FE2S_FER_2. 1 hit.
PS51384. FAD_FR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q03304-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFNIQSDDLL HHFEADSNDT LLSAALRAEL VFPYECNSGG CGACKIELLE
60 70 80 90 100
GEVSNLWPDA PGLAARELRK NRFLACQCKP LSDLKIKVIN RAEGRASHPP
110 120 130 140 150
KRFSTRVVSK RFLSDEMFEL RLEAEQKVVF SPGQYFMVDV PELGTRAYSA
160 170 180 190 200
ANPVDGNTLT LIVKAVPNGK VSCALANETI ETLQLDGPYG LSVLKTADET
210 220 230 240 250
QSVFIAGGSG IAPMVSMVNT LIAQGYEKPI TVFYGSRLEA ELEAAETLFG
260 270 280 290 300
WKENLKLINV SSSVVGNSEK KYPTGYVHEI IPEYMEGLLG AEFYLCGPPQ
310 320
MINSVQKLLM IENKVPFEAI HFDRFF
Length:326
Mass (Da):35,983
Last modified:November 1, 1995 - v1
Checksum:i17889D794FC092EE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M95045 Genomic DNA. Translation: AAA26004.1.
PIRiA47016.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M95045 Genomic DNA. Translation: AAA26004.1.
PIRiA47016.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4WQMX-ray1.62A2-326[»]
ProteinModelPortaliQ03304.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00273.

Family and domain databases

CDDicd00207. fer2. 1 hit.
Gene3Di3.10.20.30. 1 hit.
InterProiIPR001041. 2Fe-2S_ferredoxin-type.
IPR006058. 2Fe2S_fd_BS.
IPR012675. Beta-grasp_dom.
IPR017927. Fd_Rdtase_FAD-bd.
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]
PfamiPF00970. FAD_binding_6. 1 hit.
PF00111. Fer2. 1 hit.
PF00175. NAD_binding_1. 1 hit.
[Graphical view]
PRINTSiPR00371. FPNCR.
PR00410. PHEHYDRXLASE.
SUPFAMiSSF54292. SSF54292. 1 hit.
SSF63380. SSF63380. 1 hit.
PROSITEiPS00197. 2FE2S_FER_1. 1 hit.
PS51085. 2FE2S_FER_2. 1 hit.
PS51384. FAD_FR. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiTMOF_PSEME
AccessioniPrimary (citable) accession number: Q03304
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: September 7, 2016
This is version 84 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.