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Protein

Toluene-4-monooxygenase system ferredoxin subunit

Gene

tmoC

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

Functioni

Probable electron transfer from NADPH, via FAD and the 2Fe-2S center, to the oxygenase activity site of the enzyme.

Cofactori

[2Fe-2S] cluster3 PublicationsNote: Binds 1 [2Fe-2S] cluster.3 Publications

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 bindingi45 – 451Iron-sulfur (2Fe-2S)
Metal bindingi47 – 471Iron-sulfur (2Fe-2S); via pros nitrogen
Metal bindingi64 – 641Iron-sulfur (2Fe-2S)
Metal bindingi67 – 671Iron-sulfur (2Fe-2S); via pros nitrogen

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Aromatic hydrocarbons catabolism, Electron transport, Transport

Keywords - Ligandi

2Fe-2S, Iron, Iron-sulfur, Metal-binding

Enzyme and pathway databases

UniPathwayiUPA00273.

Names & Taxonomyi

Protein namesi
Recommended name:
Toluene-4-monooxygenase system ferredoxin subunit
Alternative name(s):
Toluene-4-monooxygenase system protein C
Short name:
T4moC
Gene namesi
Name:tmoC
OrganismiPseudomonas mendocina
Taxonomic identifieri300 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved
Chaini2 – 112111Toluene-4-monooxygenase system ferredoxin subunitPRO_0000072601Add
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.3 Publications

Structurei

Secondary structure

1
112
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 85Combined sources
Helixi9 – 113Combined sources
Beta strandi16 – 216Combined sources
Beta strandi27 – 337Combined sources
Turni34 – 363Combined sources
Beta strandi37 – 448Combined sources
Beta strandi46 – 494Combined sources
Helixi52 – 543Combined sources
Beta strandi55 – 584Combined sources
Beta strandi61 – 633Combined sources
Turni65 – 673Combined sources
Beta strandi70 – 723Combined sources
Turni73 – 753Combined sources
Beta strandi77 – 837Combined sources
Beta strandi91 – 944Combined sources
Beta strandi97 – 1004Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1SJGNMR-A1-112[»]
1VM9X-ray1.48A2-112[»]
2Q3WX-ray1.48A2-112[»]
4P1BX-ray2.05H/I2-112[»]
4P1CX-ray2.40H/I2-112[»]
ProteinModelPortaliQ00458.
SMRiQ00458. Positions 1-112.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ00458.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini4 – 10097RieskePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 Rieske domain.PROSITE-ProRule annotation

Family and domain databases

Gene3Di2.102.10.10. 1 hit.
InterProiIPR017941. Rieske_2Fe-2S.
[Graphical view]
PfamiPF00355. Rieske. 1 hit.
[Graphical view]
SUPFAMiSSF50022. SSF50022. 1 hit.
PROSITEiPS51296. RIESKE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q00458-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSFEKICSLD DIWVGEMETF ETSDGTEVLI VNSEEHGVKA YQAMCPHQEI
60 70 80 90 100
LLSEGSYEGG VITCRAHLWT FNDGTGHGIN PDDCCLAEYP VEVKGDDIYV
110
STKGILPNKA HS
Length:112
Mass (Da):12,326
Last modified:January 23, 2007 - v2
Checksum:iB13CD9A7FC832D07
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M65106 Genomic DNA. Translation: AAA26001.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M65106 Genomic DNA. Translation: AAA26001.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1SJGNMR-A1-112[»]
1VM9X-ray1.48A2-112[»]
2Q3WX-ray1.48A2-112[»]
4P1BX-ray2.05H/I2-112[»]
4P1CX-ray2.40H/I2-112[»]
ProteinModelPortaliQ00458.
SMRiQ00458. Positions 1-112.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00273.

Miscellaneous databases

EvolutionaryTraceiQ00458.

Family and domain databases

Gene3Di2.102.10.10. 1 hit.
InterProiIPR017941. Rieske_2Fe-2S.
[Graphical view]
PfamiPF00355. Rieske. 1 hit.
[Graphical view]
SUPFAMiSSF50022. SSF50022. 1 hit.
PROSITEiPS51296. RIESKE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiTMOC_PSEME
AccessioniPrimary (citable) accession number: Q00458
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: January 23, 2007
Last modified: October 14, 2015
This is version 72 of the entry and version 2 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.