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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)DescriptionActionsGraphical viewLength
Metal bindingi36Iron-sulfur (2Fe-2S)PROSITE-ProRule annotation1
Metal bindingi41Iron-sulfur (2Fe-2S)PROSITE-ProRule annotation1
Metal bindingi44Iron-sulfur (2Fe-2S)PROSITE-ProRule annotation1
Metal bindingi76Iron-sulfur (2Fe-2S)PROSITE-ProRule annotation1

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)DescriptionActionsGraphical viewLength
ChainiPRO_00001676581 – 326Toluene-4-monooxygenase electron transfer componentAdd BLAST326

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

1326
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi2 – 5Combined sources4
Beta strandi9 – 11Combined sources3
Beta strandi13 – 15Combined sources3
Helixi21 – 27Combined sources7
Beta strandi37 – 41Combined sources5
Beta strandi45 – 51Combined sources7
Beta strandi53 – 56Combined sources4
Helixi65 – 69Combined sources5
Beta strandi72 – 74Combined sources3
Helixi75 – 77Combined sources3
Beta strandi78 – 82Combined sources5
Beta strandi84 – 88Combined sources5
Beta strandi101 – 123Combined sources23
Beta strandi135 – 140Combined sources6
Turni141 – 143Combined sources3
Beta strandi144 – 149Combined sources6
Beta strandi158 – 164Combined sources7
Helixi170 – 177Combined sources8
Beta strandi181 – 189Combined sources9
Beta strandi202 – 207Combined sources6
Helixi208 – 210Combined sources3
Helixi211 – 223Combined sources13
Beta strandi230 – 237Combined sources8
Helixi239 – 248Combined sources10
Beta strandi255 – 261Combined sources7
Helixi277 – 280Combined sources4
Helixi281 – 288Combined sources8
Beta strandi292 – 297Combined sources6
Helixi299 – 310Combined sources12
Helixi317 – 319Combined sources3
Beta strandi320 – 324Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4WQMX-ray1.62A2-326[»]
ProteinModelPortaliQ03304.
SMRiQ03304.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 922Fe-2S ferredoxin-typePROSITE-ProRule annotationAdd BLAST92
Domaini100 – 195FAD-binding FR-typePROSITE-ProRule annotationAdd BLAST96

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni95 – 326Ferredoxin-reductaseAdd BLAST232

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4WQMX-ray1.62A2-326[»]
ProteinModelPortaliQ03304.
SMRiQ03304.
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: November 2, 2016
This is version 85 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.