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Protein

Benzene 1,2-dioxygenase system ferredoxin--NAD(+) reductase subunit

Gene

bedA

Organism
Pseudomonas putida (Arthrobacter siderocapsulatus)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Part of the electron transfer component of benzene 1,2-dioxygenase, transfers electrons from ferredoxin to NADH.

Catalytic activityi

Reduced ferredoxin + NAD+ = oxidized ferredoxin + NADH.

Cofactori

Pathwayi: benzene degradation

This protein is involved in step 1 of the subpathway that synthesizes catechol from benzene.
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Benzene 1,2-dioxygenase system ferredoxin subunit (bedB), Benzene 1,2-dioxygenase system ferredoxin subunit (bnzC), Benzene 1,2-dioxygenase subunit beta (bedC2), Benzene 1,2-dioxygenase system ferredoxin--NAD(+) reductase subunit (bedA), Benzene 1,2-dioxygenase system ferredoxin--NAD(+) reductase component (bnzD), Benzene 1,2-dioxygenase subunit alpha (bedC1), Benzene 1,2-dioxygenase subunit beta (bnzB), Benzene 1,2-dioxygenase subunit alpha (bnzA)
  2. Cis-1,2-dihydrobenzene-1,2-diol dehydrogenase (bnzE)
This subpathway is part of the pathway benzene degradation, which is itself part of Aromatic compound metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes catechol from benzene, the pathway benzene degradation and in Aromatic compound metabolism.

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-12882.
UniPathwayiUPA00272; UER00391.

Names & Taxonomyi

Protein namesi
Recommended name:
Benzene 1,2-dioxygenase system ferredoxin--NAD(+) reductase subunit (EC:1.18.1.3)
Gene namesi
Name:bedA
Encoded oniPlasmid pHMT1120 Publication
OrganismiPseudomonas putida (Arthrobacter siderocapsulatus)
Taxonomic identifieri303 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 410410Benzene 1,2-dioxygenase system ferredoxin--NAD(+) reductase subunitPRO_0000167652Add
BLAST

Interactioni

Subunit structurei

This dioxygenase system consists of four proteins: the two subunits of the hydroxylase component (BedC1 and BedC2), a ferredoxin (BedB) and a ferredoxin reductase (BedA).

Structurei

3D structure databases

ProteinModelPortaliQ07946.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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.

Q07946-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MANHVAIIGN GVAGFTTAQA LRAEGYEGRI SLIGEEQHLP YDRPSLSKAV
60 70 80 90 100
LDGSFEQPPR LAEADWYSEA SIEMLTGSEV TDLDTQKKMI SLNDGSTISA
110 120 130 140 150
DAIVIATGSR ARMLSLPGSQ LPGVVTLRTY GDVQLLRDSW TPNTRLLIVG
160 170 180 190 200
GGLIGCEVAT TARKLGLSVT ILEAGDELLV RVLGRRIGAW LRGLLTEQGV
210 220 230 240 250
QVELKTGVSG FSGEGQLEKV MVNDGRSFIA DNALICVGAD PADQLARQAG
260 270 280 290 300
LECDRGVVVD HRGATSAKGI FAVGDVATWP LHSGGKRSLE TYMNAQRQAT
310 320 330 340 350
AVAKAILGKE VSAPQLPVSW TEIAGHRMQM AGDIEGPGEY VLRGTLGIGS
360 370 380 390 400
ALLFRLLDGR IQAVVAVDAP RDFALANRLV EAQVIIEPEK LADVSNNMRD
410
IVRANEGNQK
Length:410
Mass (Da):43,587
Last modified:November 1, 1995 - v1
Checksum:i1852467DC01D41EA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF148496 Genomic DNA. Translation: AAA17761.1.
PIRiJN0810.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF148496 Genomic DNA. Translation: AAA17761.1.
PIRiJN0810.

3D structure databases

ProteinModelPortaliQ07946.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00272; UER00391.
BioCyciMetaCyc:MONOMER-12882.

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...

Publicationsi

  1. "The Pseudomonas putida ML2 plasmid-encoded genes for benzene dioxygenase are unusual in codon usage and low in G+C content."
    Tan H.-M., Tang H.-Y., Joannou C., Abdel-Wahab N.H., Mason J.R.
    Gene 130:33-39(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 3-14.
    Strain: ML2.

Entry informationi

Entry nameiBEDA_PSEPU
AccessioniPrimary (citable) accession number: Q07946
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: May 11, 2016
This is version 83 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

Direct protein sequencing, Plasmid

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. 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.