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Protein

Oxygen-insensitive NAD(P)H nitroreductase

Gene

nfsB

Organism
Enterobacter cloacae
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Reduction of a variety of nitroaromatic compounds using NADH (and to lesser extent NADPH) as source of reducing equivalents; two electrons are transferred.

Cofactori

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei41NAD or NADP; via amide nitrogenCurated1
Binding sitei71FMN1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi10 – 14FMN5
Nucleotide bindingi153 – 158NAD or NADPBy similarity6
Nucleotide bindingi165 – 166FMN2
Nucleotide bindingi205 – 207FMN3

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Flavoprotein, FMN, NAD, NADP

Names & Taxonomyi

Protein namesi
Recommended name:
Oxygen-insensitive NAD(P)H nitroreductase (EC:1.-.-.-)
Short name:
NR
Gene namesi
Name:nfsBBy similarity
Synonyms:nfnB, nfsIImported
OrganismiEnterobacter cloacae
Taxonomic identifieri550 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEnterobacterEnterobacter cloacae complex

Pathology & Biotechi

Chemistry databases

DrugBankiDB03793. Benzoic Acid.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000727121 – 217Oxygen-insensitive NAD(P)H nitroreductaseAdd BLAST217

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

STRINGi716541.ECL_03157.

Structurei

Secondary structure

1217
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi3 – 9Combined sources7
Helixi24 – 36Combined sources13
Helixi40 – 42Combined sources3
Beta strandi46 – 51Combined sources6
Helixi54 – 60Combined sources7
Helixi61 – 63Combined sources3
Helixi66 – 71Combined sources6
Helixi72 – 77Combined sources6
Beta strandi78 – 89Combined sources12
Helixi92 – 104Combined sources13
Helixi111 – 129Combined sources19
Turni130 – 132Combined sources3
Helixi135 – 156Combined sources22
Helixi169 – 175Combined sources7
Helixi178 – 181Combined sources4
Beta strandi183 – 192Combined sources10
Helixi199 – 201Combined sources3
Helixi210 – 213Combined sources4
Beta strandi214 – 217Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1KQBX-ray1.80A/B/C/D1-217[»]
1KQCX-ray1.80A/B/C/D1-217[»]
1KQDX-ray1.90A/B/C/D1-217[»]
1NECX-ray1.95A/B/C/D2-217[»]
ProteinModelPortaliQ01234.
SMRiQ01234.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ01234.

Family & Domainsi

Sequence similaritiesi

Belongs to the nitroreductase family.Curated

Phylogenomic databases

eggNOGiENOG4108RCM. Bacteria.
COG0778. LUCA.

Family and domain databases

CDDicd02149. NfsB_like_nitroreductase. 1 hit.
Gene3Di3.40.109.10. 1 hit.
InterProiIPR033878. NfsB-like.
IPR029479. Nitroreductase.
IPR000415. Nitroreductase-like.
[Graphical view]
PfamiPF00881. Nitroreductase. 1 hit.
[Graphical view]
SUPFAMiSSF55469. SSF55469. 1 hit.

Sequencei

Sequence statusi: Complete.

Q01234-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDIISVALKR HSTKAFDASK KLTAEEAEKI KTLLQYSPSS TNSQPWHFIV
60 70 80 90 100
ASTEEGKARV AKSAAGTYVF NERKMLDASH VVVFCAKTAM DDAWLERVVD
110 120 130 140 150
QEEADGRFNT PEAKAANHKG RTYFADMHRV DLKDDDQWMA KQVYLNVGNF
160 170 180 190 200
LLGVGAMGLD AVPIEGFDAA ILDEEFGLKE KGFTSLVVVP VGHHSVEDFN
210
ATLPKSRLPL STIVTEC
Length:217
Mass (Da):23,950
Last modified:July 1, 1993 - v1
Checksum:iC42AA3DB184D5D9B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M63808 Genomic DNA. Translation: AAA62801.1.
PIRiA38686.
RefSeqiWP_024906901.1. NZ_JWCB01000014.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M63808 Genomic DNA. Translation: AAA62801.1.
PIRiA38686.
RefSeqiWP_024906901.1. NZ_JWCB01000014.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1KQBX-ray1.80A/B/C/D1-217[»]
1KQCX-ray1.80A/B/C/D1-217[»]
1KQDX-ray1.90A/B/C/D1-217[»]
1NECX-ray1.95A/B/C/D2-217[»]
ProteinModelPortaliQ01234.
SMRiQ01234.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi716541.ECL_03157.

Chemistry databases

DrugBankiDB03793. Benzoic Acid.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4108RCM. Bacteria.
COG0778. LUCA.

Miscellaneous databases

EvolutionaryTraceiQ01234.

Family and domain databases

CDDicd02149. NfsB_like_nitroreductase. 1 hit.
Gene3Di3.40.109.10. 1 hit.
InterProiIPR033878. NfsB-like.
IPR029479. Nitroreductase.
IPR000415. Nitroreductase-like.
[Graphical view]
PfamiPF00881. Nitroreductase. 1 hit.
[Graphical view]
SUPFAMiSSF55469. SSF55469. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiNFSB_ENTCL
AccessioniPrimary (citable) accession number: Q01234
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: November 30, 2016
This is version 76 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

The nitroreductase might be involved in the quinone metabolism.

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  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.