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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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei73 – 731FMN

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi12 – 165FMN
Nucleotide bindingi154 – 1596NAD or NADPBy similarity
Nucleotide bindingi165 – 1662FMN
Nucleotide bindingi206 – 2083FMN

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)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved
Chaini2 – 218217Major NAD(P)H-flavin oxidoreductasePRO_0000072714Add
BLAST

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

STRINGi312309.VF_A0691.

Structurei

Secondary structure

1
218
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 118Combined sources
Beta strandi16 – 183Combined sources
Helixi26 – 3712Combined sources
Helixi42 – 443Combined sources
Beta strandi48 – 536Combined sources
Helixi56 – 649Combined sources
Beta strandi67 – 693Combined sources
Helixi71 – 755Combined sources
Helixi76 – 794Combined sources
Beta strandi80 – 9011Combined sources
Helixi94 – 10613Combined sources
Helixi112 – 1187Combined sources
Helixi119 – 1224Combined sources
Helixi123 – 1275Combined sources
Beta strandi131 – 1333Combined sources
Helixi136 – 15722Combined sources
Beta strandi160 – 1645Combined sources
Helixi169 – 1757Combined sources
Turni176 – 1827Combined sources
Beta strandi183 – 19210Combined sources
Turni196 – 1983Combined sources
Helixi200 – 2034Combined sources
Helixi211 – 2144Combined sources
Beta strandi215 – 2173Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1V5YX-ray1.90A/B2-218[»]
1V5ZX-ray2.00A/B2-218[»]
1VFRX-ray1.80A/B1-218[»]
ProteinModelPortaliP46072.
SMRiP46072. Positions 2-218.
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

Gene3Di3.40.109.10. 1 hit.
InterProiIPR029479. 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
EntryMethodResolution (Å)ChainPositionsPDBsum
1V5YX-ray1.90A/B2-218[»]
1V5ZX-ray2.00A/B2-218[»]
1VFRX-ray1.80A/B1-218[»]
ProteinModelPortaliP46072.
SMRiP46072. Positions 2-218.
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

Gene3Di3.40.109.10. 1 hit.
InterProiIPR029479. 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 11, 2015
This is version 74 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.