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Protein

FMN reductase (NADPH)

Gene

ssuE

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes an NADPH-dependent reduction of FMN, but is also able to reduce FAD or riboflavin.

Catalytic activityi

FMNH2 + NADP+ = FMN + NADPH.

GO - Molecular functioni

  • FMN reductase (NADPH) activity Source: UniProtKB-EC
  • FMN reductase activity Source: EcoCyc

GO - Biological processi

  • alkanesulfonate catabolic process Source: EcoCyc
  • cellular response to DNA damage stimulus Source: EcoliWiki
  • cellular response to sulfate starvation Source: EcoCyc
  • protein homotetramerization Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Flavoprotein, FMN, NADP

Enzyme and pathway databases

BioCyciEcoCyc:MONOMER0-146.
ECOL316407:JW0920-MONOMER.
MetaCyc:MONOMER0-146.
BRENDAi1.5.1.38. 2026.

Names & Taxonomyi

Protein namesi
Recommended name:
FMN reductase (NADPH) (EC:1.5.1.38)
Alternative name(s):
FMN reductase
Sulfate starvation-induced protein 4
Short name:
SSI4
Gene namesi
Name:ssuE
Synonyms:ycbP
Ordered Locus Names:b0937, JW0920
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG13708. ssuE.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 191191FMN reductase (NADPH)PRO_0000160591Add
BLAST

Proteomic databases

PaxDbiP80644.

Expressioni

Inductioni

Repressed by sulfate or cysteine.

Interactioni

Subunit structurei

Homodimer.

Binary interactionsi

WithEntry#Exp.IntActNotes
ssuDP806452EBI-1121047,EBI-561637

Protein-protein interaction databases

BioGridi4262118. 25 interactions.
DIPiDIP-10929N.
IntActiP80644. 5 interactions.
STRINGi511145.b0937.

Structurei

Secondary structure

1
191
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 76Combined sources
Beta strandi10 – 134Combined sources
Helixi15 – 2915Combined sources
Beta strandi33 – 386Combined sources
Helixi39 – 413Combined sources
Helixi44 – 485Combined sources
Helixi55 – 6612Combined sources
Beta strandi68 – 758Combined sources
Helixi83 – 908Combined sources
Turni94 – 996Combined sources
Beta strandi101 – 11010Combined sources
Helixi111 – 1155Combined sources
Helixi116 – 1194Combined sources
Helixi121 – 1277Combined sources
Beta strandi131 – 1344Combined sources
Beta strandi137 – 1404Combined sources
Helixi141 – 1433Combined sources
Beta strandi144 – 1507Combined sources
Helixi155 – 17218Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4PTYX-ray2.10A/B/C/D1-191[»]
4PTZX-ray1.90A/B/C/D1-191[»]
4PU0X-ray2.30A/B/C/D1-191[»]
ProteinModelPortaliP80644.
SMRiP80644. Positions 1-175.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the SsuE family.Curated

Phylogenomic databases

eggNOGiENOG4108UZX. Bacteria.
COG0431. LUCA.
HOGENOMiHOG000263120.
InParanoidiP80644.
KOiK00299.
OMAiARFDSPQ.
PhylomeDBiP80644.

Family and domain databases

Gene3Di3.40.50.360. 1 hit.
InterProiIPR029039. Flavoprotein-like_dom.
IPR005025. FMN_Rdtase-like.
IPR020048. NADPH-dep_FMN_reduc_SsuE.
[Graphical view]
PfamiPF03358. FMN_red. 1 hit.
[Graphical view]
SUPFAMiSSF52218. SSF52218. 1 hit.
TIGRFAMsiTIGR03567. FMN_reduc_SsuE. 1 hit.

Sequencei

Sequence statusi: Complete.

P80644-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRVITLAGSP RFPSRSSSLL EYAREKLNGL DVEVYHWNLQ NFAPEDLLYA
60 70 80 90 100
RFDSPALKTF TEQLQQADGL IVATPVYKAA YSGALKTLLD LLPERALQGK
110 120 130 140 150
VVLPLATGGT VAHLLAVDYA LKPVLSALKA QEILHGVFAD DSQVIDYHHR
160 170 180 190
PQFTPNLQTR LDTALETFWQ ALHRRDVQVP DLLSLRGNAH A
Length:191
Mass (Da):21,253
Last modified:November 1, 1997 - v2
Checksum:i2371808C97CEE532
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ237695 Genomic DNA. Translation: CAB40389.1.
U00096 Genomic DNA. Translation: AAC74023.1.
AP009048 Genomic DNA. Translation: BAA35692.1.
PIRiH64833.
RefSeqiNP_415457.1. NC_000913.3.
WP_001263933.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC74023; AAC74023; b0937.
BAA35692; BAA35692; BAA35692.
GeneIDi945947.
KEGGiecj:JW0920.
eco:b0937.
PATRICi32117093. VBIEscCol129921_0971.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ237695 Genomic DNA. Translation: CAB40389.1.
U00096 Genomic DNA. Translation: AAC74023.1.
AP009048 Genomic DNA. Translation: BAA35692.1.
PIRiH64833.
RefSeqiNP_415457.1. NC_000913.3.
WP_001263933.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4PTYX-ray2.10A/B/C/D1-191[»]
4PTZX-ray1.90A/B/C/D1-191[»]
4PU0X-ray2.30A/B/C/D1-191[»]
ProteinModelPortaliP80644.
SMRiP80644. Positions 1-175.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262118. 25 interactions.
DIPiDIP-10929N.
IntActiP80644. 5 interactions.
STRINGi511145.b0937.

Proteomic databases

PaxDbiP80644.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74023; AAC74023; b0937.
BAA35692; BAA35692; BAA35692.
GeneIDi945947.
KEGGiecj:JW0920.
eco:b0937.
PATRICi32117093. VBIEscCol129921_0971.

Organism-specific databases

EchoBASEiEB3472.
EcoGeneiEG13708. ssuE.

Phylogenomic databases

eggNOGiENOG4108UZX. Bacteria.
COG0431. LUCA.
HOGENOMiHOG000263120.
InParanoidiP80644.
KOiK00299.
OMAiARFDSPQ.
PhylomeDBiP80644.

Enzyme and pathway databases

BioCyciEcoCyc:MONOMER0-146.
ECOL316407:JW0920-MONOMER.
MetaCyc:MONOMER0-146.
BRENDAi1.5.1.38. 2026.

Miscellaneous databases

PROiP80644.

Family and domain databases

Gene3Di3.40.50.360. 1 hit.
InterProiIPR029039. Flavoprotein-like_dom.
IPR005025. FMN_Rdtase-like.
IPR020048. NADPH-dep_FMN_reduc_SsuE.
[Graphical view]
PfamiPF03358. FMN_red. 1 hit.
[Graphical view]
SUPFAMiSSF52218. SSF52218. 1 hit.
TIGRFAMsiTIGR03567. FMN_reduc_SsuE. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiSSUE_ECOLI
AccessioniPrimary (citable) accession number: P80644
Secondary accession number(s): P75854
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: November 1, 1997
Last modified: September 7, 2016
This is version 119 of the entry and version 2 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, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  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.