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Protein
Submitted name:

NADH:flavin oxidoreductase Sye1

Gene

sye1

Organism
Shewanella oneidensis (strain MR-1)
Status
Unreviewed-Annotation score: Annotation score: 1 out of 5-Experimental evidence at protein leveli

Functioni

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei58 – 581FMN; via amide nitrogenCombined sources
Binding sitei100 – 1001FMNCombined sources
Binding sitei181 – 1811FMNCombined sources
Binding sitei233 – 2331FMNCombined sources
Binding sitei274 – 2741FMNCombined sources
Binding sitei301 – 3011FMN; via amide nitrogenCombined sources

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi24 – 263FMNCombined sources
Nucleotide bindingi322 – 3232FMNCombined sources

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

Flavoprotein, FMNCombined sources, Nucleotide-bindingCombined sources

Names & Taxonomyi

Protein namesi
Submitted name:
NADH:flavin oxidoreductase Sye1Imported
Gene namesi
Name:sye1Imported
Ordered Locus Names:SO_2454Imported
OrganismiShewanella oneidensis (strain MR-1)Imported
Taxonomic identifieri211586 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesShewanellaceaeShewanella
Proteomesi
  • UP000008186 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Proteomic databases

PaxDbiQ8EEC8.

Interactioni

Protein-protein interaction databases

STRINGi211586.SO_2454.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2GOUX-ray1.40A1-365[»]
2GQ8X-ray1.70A1-365[»]
2GQ9X-ray1.70A1-365[»]
2GQAX-ray1.70A1-365[»]
4AWSX-ray1.00A1-365[»]
4AWTX-ray0.98A1-365[»]
4AWUX-ray1.69A1-365[»]
ProteinModelPortaliQ8EEC8.
SMRiQ8EEC8. Positions 1-365.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8EEC8.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini4 – 341338Oxidored_FMNInterPro annotationAdd
BLAST

Phylogenomic databases

eggNOGiENOG4105CCY. Bacteria.
COG1902. LUCA.
HOGENOMiHOG000116231.
KOiK10680.
OMAiIVYLHIA.
OrthoDBiEOG6XWTZX.
PhylomeDBiQ8EEC8.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR001155. OxRdtase_FMN_N.
[Graphical view]
PfamiPF00724. Oxidored_FMN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8EEC8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTQSLFQPIT LGALTLKNRI VMPPMTRSRA SQPGDVANHM MAIYYAQRAS
60 70 80 90 100
AGLIVSEGTQ ISPTAKGYAW TPGIYTPEQI AGWRIVTEAV HAKGCAIFAQ
110 120 130 140 150
LWHVGRVTHP DNIDGQQPIS SSTLKAENVK VFVDNGSDEP GFVDVAVPRA
160 170 180 190 200
MTKADIAQVI ADYRQAALNA MEAGFDGIEL HAANGYLINQ FIDSEANNRS
210 220 230 240 250
DEYGGSLENR LRFLDEVVAA LVDAIGAERV GVRLAPLTTL NGTVDADPIL
260 270 280 290 300
TYTAAAALLN KHRIVYLHIA EVDWDDAPDT PVSFKRALRE AYQGVLIYAG
310 320 330 340 350
RYNAEKAEQA INDGLADMIG FGRPFIANPD LPERLRHGYP LAEHVPATLF
360
GGGEKGLTDY PTYQA
Length:365
Mass (Da):39,593
Last modified:March 1, 2003 - v1
Checksum:iD2B109AF91C2879B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014299 Genomic DNA. Translation: AAN55488.1.
RefSeqiNP_718044.1. NC_004347.2.
WP_011072430.1. NC_004347.2.

Genome annotation databases

EnsemblBacteriaiAAN55488; AAN55488; SO_2454.
GeneIDi1170169.
KEGGison:SO_2454.
PATRICi23524525. VBISheOne101494_2362.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014299 Genomic DNA. Translation: AAN55488.1.
RefSeqiNP_718044.1. NC_004347.2.
WP_011072430.1. NC_004347.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2GOUX-ray1.40A1-365[»]
2GQ8X-ray1.70A1-365[»]
2GQ9X-ray1.70A1-365[»]
2GQAX-ray1.70A1-365[»]
4AWSX-ray1.00A1-365[»]
4AWTX-ray0.98A1-365[»]
4AWUX-ray1.69A1-365[»]
ProteinModelPortaliQ8EEC8.
SMRiQ8EEC8. Positions 1-365.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi211586.SO_2454.

Proteomic databases

PaxDbiQ8EEC8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAN55488; AAN55488; SO_2454.
GeneIDi1170169.
KEGGison:SO_2454.
PATRICi23524525. VBISheOne101494_2362.

Phylogenomic databases

eggNOGiENOG4105CCY. Bacteria.
COG1902. LUCA.
HOGENOMiHOG000116231.
KOiK10680.
OMAiIVYLHIA.
OrthoDBiEOG6XWTZX.
PhylomeDBiQ8EEC8.

Miscellaneous databases

EvolutionaryTraceiQ8EEC8.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR001155. OxRdtase_FMN_N.
[Graphical view]
PfamiPF00724. Oxidored_FMN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: MR-1Imported.
  2. "Ligand-induced conformational changes in the capping subdomain of a bacterial old yellow enzyme homologue and conserved sequence fingerprints provide new insights into substrate binding."
    van den Hemel D., Brige A., Savvides S.N., Van Beeumen J.
    J. Biol. Chem. 281:28152-28161(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) IN COMPLEX WITH FMN.
  3. "Modulation of Isoalloxazine Ring Planarity Influences Fmn Electronic Properties in Old Yellow Enzymes."
    Elegheert J., Pauwels E., Wille G., Brige A., Savvides S.N.
    Submitted (JUN-2012) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.00 ANGSTROMS) IN COMPLEX WITH FMN, X-RAY CRYSTALLOGRAPHY (0.98 ANGSTROMS) IN COMPLEX WITH FMN, X-RAY CRYSTALLOGRAPHY (1.69 ANGSTROMS) IN COMPLEX WITH FMN.

Entry informationi

Entry nameiQ8EEC8_SHEON
AccessioniPrimary (citable) accession number: Q8EEC8
Entry historyi
Integrated into UniProtKB/TrEMBL: March 1, 2003
Last sequence update: March 1, 2003
Last modified: April 13, 2016
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources, Complete proteome, Reference proteomeImported

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.