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Protein

Toluene 1,2-dioxygenase system ferredoxin--NAD(+) reductase component

Gene

todA

Organism
Pseudomonas putida (strain ATCC 700007 / DSM 6899 / BCRC 17059 / F1)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Part of the electron transfer component of toluene 1,2-dioxygenase, transfers electrons from ferredoxin (TodB) to NADH.

Catalytic activityi

Reduced ferredoxin + NAD+ = oxidized ferredoxin + NADH.

Cofactori

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.

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi4 – 35FADSequence analysisAdd BLAST32
Nucleotide bindingi145 – 173NADSequence analysisAdd BLAST29

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Aromatic hydrocarbons catabolism

Keywords - Ligandi

FAD, Flavoprotein, NAD

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-11350.
UniPathwayiUPA00273.

Names & Taxonomyi

Protein namesi
Recommended name:
Toluene 1,2-dioxygenase system ferredoxin--NAD(+) reductase component (EC:1.18.1.3)
Gene namesi
Name:todA
Ordered Locus Names:Pput_2878
OrganismiPseudomonas putida (strain ATCC 700007 / DSM 6899 / BCRC 17059 / F1)
Taxonomic identifieri351746 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
Proteomesi
  • UP000006553 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00003144682 – 410Toluene 1,2-dioxygenase system ferredoxin--NAD(+) reductase componentAdd BLAST409

Interactioni

Subunit structurei

This dioxygenase system consists of four proteins: the two subunits of the hydroxylase component (todC1 and todC2), a ferredoxin (TodB) and a ferredoxin reductase (TodA).

Protein-protein interaction databases

STRINGi351746.Pput_2878.

Structurei

Secondary structure

1410
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 8Combined sources5
Helixi12 – 23Combined sources12
Beta strandi28 – 34Combined sources7
Beta strandi36 – 41Combined sources6
Helixi44 – 47Combined sources4
Turni48 – 53Combined sources6
Beta strandi54 – 57Combined sources4
Beta strandi60 – 62Combined sources3
Helixi66 – 69Combined sources4
Beta strandi73 – 77Combined sources5
Beta strandi80 – 84Combined sources5
Turni85 – 88Combined sources4
Beta strandi89 – 92Combined sources4
Beta strandi97 – 99Combined sources3
Beta strandi101 – 105Combined sources5
Beta strandi109 – 111Combined sources3
Turni117 – 120Combined sources4
Helixi130 – 139Combined sources10
Beta strandi145 – 149Combined sources5
Helixi153 – 164Combined sources12
Beta strandi168 – 172Combined sources5
Beta strandi174 – 179Combined sources6
Helixi180 – 183Combined sources4
Helixi185 – 198Combined sources14
Beta strandi201 – 203Combined sources3
Beta strandi208 – 212Combined sources5
Beta strandi214 – 216Combined sources3
Beta strandi219 – 222Combined sources4
Beta strandi227 – 229Combined sources3
Beta strandi231 – 235Combined sources5
Beta strandi239 – 241Combined sources3
Helixi244 – 248Combined sources5
Beta strandi253 – 258Combined sources6
Beta strandi270 – 272Combined sources3
Helixi274 – 276Combined sources3
Beta strandi277 – 281Combined sources5
Beta strandi284 – 287Combined sources4
Helixi292 – 306Combined sources15
Beta strandi318 – 323Combined sources6
Beta strandi326 – 332Combined sources7
Beta strandi334 – 344Combined sources11
Beta strandi348 – 357Combined sources10
Beta strandi360 – 368Combined sources9
Helixi370 – 382Combined sources13
Helixi388 – 392Combined sources5
Helixi398 – 400Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3EF6X-ray1.80A1-410[»]
4EMIX-ray1.81A1-410[»]
4EMJX-ray2.40A1-410[»]
ProteinModelPortaliA5W4E9.
SMRiA5W4E9.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiA5W4E9.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4108EQM. Bacteria.
COG0446. LUCA.
HOGENOMiHOG000276711.
KOiK18090.
OMAiGNTINGW.

Family and domain databases

Gene3Di3.30.390.30. 1 hit.
3.50.50.60. 2 hits.
InterProiIPR023753. FAD/NAD-binding_dom.
IPR016156. FAD/NAD-linked_Rdtase_dimer.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
IPR028202. Reductase_C.
[Graphical view]
PfamiPF07992. Pyr_redox_2. 1 hit.
PF14759. Reductase_C. 1 hit.
[Graphical view]
SUPFAMiSSF51905. SSF51905. 2 hits.
SSF55424. SSF55424. 1 hit.

Sequencei

Sequence statusi: Complete.

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

A5W4E9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATHVAIIGN GVGGFTTAQA LRAEGFEGRI SLIGDEPHLP YDRPSLSKAV
60 70 80 90 100
LDGSLERPPI LAEADWYGEA RIDMLTGPEV TALDVQTRTI SLDDGTTLSA
110 120 130 140 150
DAIVIATGSR ARTMALPGSQ LPGVVTLRTY GDVQVLRDSW TSATRLLIVG
160 170 180 190 200
GGLIGCEVAT TARKLGLSVT ILEAGDELLV RVLGRRIGAW LRGLLTELGV
210 220 230 240 250
QVELGTGVVG FSGEGQLEQV MASDGRSFVA DSALICVGAE PADQLARQAG
260 270 280 290 300
LACDRGVIVD HCGATLAKGV FAVGDVASWP LRAGGRRSLE TYMNAQRQAA
310 320 330 340 350
AVAAAILGKN VSAPQLPVSW TEIAGHRMQM AGDIEGPGDF VSRGMPGSGA
360 370 380 390 400
ALLFRLQERR IQAVVAVDAP RDFALATRLV EARAAIEPAR LADLSNSMRD
410
FVRANEGDLT
Length:410
Mass (Da):42,942
Last modified:July 10, 2007 - v1
Checksum:i934CF2EDD2AB1450
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J04996 Genomic DNA. Translation: AAA26008.1.
CP000712 Genomic DNA. Translation: ABQ79009.1.
PIRiD36516.
RefSeqiWP_012052598.1. NC_009512.1.

Genome annotation databases

EnsemblBacteriaiABQ79009; ABQ79009; Pput_2878.
KEGGippf:Pput_2878.
PATRICi19921899. VBIPsePut56420_2934.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J04996 Genomic DNA. Translation: AAA26008.1.
CP000712 Genomic DNA. Translation: ABQ79009.1.
PIRiD36516.
RefSeqiWP_012052598.1. NC_009512.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3EF6X-ray1.80A1-410[»]
4EMIX-ray1.81A1-410[»]
4EMJX-ray2.40A1-410[»]
ProteinModelPortaliA5W4E9.
SMRiA5W4E9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi351746.Pput_2878.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABQ79009; ABQ79009; Pput_2878.
KEGGippf:Pput_2878.
PATRICi19921899. VBIPsePut56420_2934.

Phylogenomic databases

eggNOGiENOG4108EQM. Bacteria.
COG0446. LUCA.
HOGENOMiHOG000276711.
KOiK18090.
OMAiGNTINGW.

Enzyme and pathway databases

UniPathwayiUPA00273.
BioCyciMetaCyc:MONOMER-11350.

Miscellaneous databases

EvolutionaryTraceiA5W4E9.

Family and domain databases

Gene3Di3.30.390.30. 1 hit.
3.50.50.60. 2 hits.
InterProiIPR023753. FAD/NAD-binding_dom.
IPR016156. FAD/NAD-linked_Rdtase_dimer.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
IPR028202. Reductase_C.
[Graphical view]
PfamiPF07992. Pyr_redox_2. 1 hit.
PF14759. Reductase_C. 1 hit.
[Graphical view]
SUPFAMiSSF51905. SSF51905. 2 hits.
SSF55424. SSF55424. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiTODA_PSEP1
AccessioniPrimary (citable) accession number: A5W4E9
Secondary accession number(s): P13452
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: July 10, 2007
Last modified: November 2, 2016
This is version 63 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, Complete proteome, 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.