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Protein

Major NAD(P)H-flavin oxidoreductase

Gene
N/A
Organism
Aliivibrio fischeri (Vibrio fischeri)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Involved in bioluminescence. It is a good supplier of reduced flavin mononucleotide (FMNH2) to the bioluminescence reaction. Major FMN reductase. It is capable of using both NADH and NADPH as electron donors. As electron acceptor, FMN is the most effective, FAD is considerably effective, and riboflavin is the least effective.

Cofactori

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei73FMN1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi12 – 16FMN5
Nucleotide bindingi154 – 159NAD or NADPBy similarity6
Nucleotide bindingi165 – 166FMN2
Nucleotide bindingi206 – 208FMN3

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Luminescence

Keywords - Ligandi

FAD, Flavoprotein, FMN, NAD, NADP

Names & Taxonomyi

Protein namesi
Recommended name:
Major NAD(P)H-flavin oxidoreductase (EC:1.6.99.-)
Alternative name(s):
FRASE I
OrganismiAliivibrio fischeri (Vibrio fischeri)
Taxonomic identifieri668 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeAliivibrio

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved
ChainiPRO_00000727142 – 218Major NAD(P)H-flavin oxidoreductaseAdd BLAST217

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

STRINGi312309.VF_A0691.

Structurei

Secondary structure

1218
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi4 – 11Combined sources8
Beta strandi16 – 18Combined sources3
Helixi26 – 37Combined sources12
Helixi42 – 44Combined sources3
Beta strandi48 – 53Combined sources6
Helixi56 – 64Combined sources9
Beta strandi67 – 69Combined sources3
Helixi71 – 75Combined sources5
Helixi76 – 79Combined sources4
Beta strandi80 – 90Combined sources11
Helixi94 – 106Combined sources13
Helixi112 – 118Combined sources7
Helixi119 – 122Combined sources4
Helixi123 – 127Combined sources5
Beta strandi131 – 133Combined sources3
Helixi136 – 157Combined sources22
Beta strandi160 – 164Combined sources5
Helixi169 – 175Combined sources7
Turni176 – 182Combined sources7
Beta strandi183 – 192Combined sources10
Turni196 – 198Combined sources3
Helixi200 – 203Combined sources4
Helixi211 – 214Combined sources4
Beta strandi215 – 217Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1V5YX-ray1.90A/B2-218[»]
1V5ZX-ray2.00A/B2-218[»]
1VFRX-ray1.80A/B1-218[»]
ProteinModelPortaliP46072.
SMRiP46072.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP46072.

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.

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

P46072-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTHPIIHDLE NRYTSKKYDP SKKVSQEDLA VLLEALRLSA SSINSQPWKF
60 70 80 90 100
IVIESDAAKQ RMHDSFANMH QFNQPHIKAC SHVILFANKL SYTRDDYDVV
110 120 130 140 150
LSKAVADKRI TEEQKEAAFA SFKFVELNCD ENGEHKAWTK PQAYLALGNA
160 170 180 190 200
LHTLARLNID STTMEGIDPE LLSEIFADEL KGYECHVALA IGYHHPSEDY
210
NASLPKSRKA FEDVITIL
Length:218
Mass (Da):24,721
Last modified:January 23, 2007 - v3
Checksum:iAC223CF8CEE5A636
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D17743 Genomic DNA. Translation: BAA04595.2.
PIRiS46241.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D17743 Genomic DNA. Translation: BAA04595.2.
PIRiS46241.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1V5YX-ray1.90A/B2-218[»]
1V5ZX-ray2.00A/B2-218[»]
1VFRX-ray1.80A/B1-218[»]
ProteinModelPortaliP46072.
SMRiP46072.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi312309.VF_A0691.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4108RCM. Bacteria.
COG0778. LUCA.

Miscellaneous databases

EvolutionaryTraceiP46072.

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 nameiFRA1_ALIFS
AccessioniPrimary (citable) accession number: P46072
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: January 23, 2007
Last modified: November 30, 2016
This is version 77 of the entry and version 3 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. 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.