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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)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi4 – 3532FADSequence analysisAdd
BLAST
Nucleotide bindingi145 – 17329NADSequence analysisAdd
BLAST

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.
PPUT351746:GI26-2926-MONOMER.
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)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 410409Toluene 1,2-dioxygenase system ferredoxin--NAD(+) reductase componentPRO_0000314468Add
BLAST

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

1
410
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 85Combined sources
Helixi12 – 2312Combined sources
Beta strandi28 – 347Combined sources
Beta strandi36 – 416Combined sources
Helixi44 – 474Combined sources
Turni48 – 536Combined sources
Beta strandi54 – 574Combined sources
Beta strandi60 – 623Combined sources
Helixi66 – 694Combined sources
Beta strandi73 – 775Combined sources
Beta strandi80 – 845Combined sources
Turni85 – 884Combined sources
Beta strandi89 – 924Combined sources
Beta strandi97 – 993Combined sources
Beta strandi101 – 1055Combined sources
Beta strandi109 – 1113Combined sources
Turni117 – 1204Combined sources
Helixi130 – 13910Combined sources
Beta strandi145 – 1495Combined sources
Helixi153 – 16412Combined sources
Beta strandi168 – 1725Combined sources
Beta strandi174 – 1796Combined sources
Helixi180 – 1834Combined sources
Helixi185 – 19814Combined sources
Beta strandi201 – 2033Combined sources
Beta strandi208 – 2125Combined sources
Beta strandi214 – 2163Combined sources
Beta strandi219 – 2224Combined sources
Beta strandi227 – 2293Combined sources
Beta strandi231 – 2355Combined sources
Beta strandi239 – 2413Combined sources
Helixi244 – 2485Combined sources
Beta strandi253 – 2586Combined sources
Beta strandi270 – 2723Combined sources
Helixi274 – 2763Combined sources
Beta strandi277 – 2815Combined sources
Beta strandi284 – 2874Combined sources
Helixi292 – 30615Combined sources
Beta strandi318 – 3236Combined sources
Beta strandi326 – 3327Combined sources
Beta strandi334 – 34411Combined sources
Beta strandi348 – 35710Combined sources
Beta strandi360 – 3689Combined sources
Helixi370 – 38213Combined sources
Helixi388 – 3925Combined sources
Helixi398 – 4003Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3EF6X-ray1.80A1-410[»]
4EMIX-ray1.81A1-410[»]
4EMJX-ray2.40A1-410[»]
ProteinModelPortaliA5W4E9.
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
EntryMethodResolution (Å)ChainPositionsPDBsum
3EF6X-ray1.80A1-410[»]
4EMIX-ray1.81A1-410[»]
4EMJX-ray2.40A1-410[»]
ProteinModelPortaliA5W4E9.
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.
PPUT351746:GI26-2926-MONOMER.

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: September 7, 2016
This is version 61 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.