Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein
Submitted name:

Fructosyl amine: oxygen oxidoreductase

Gene
N/A
Organism
Neosartorya fumigata (Aspergillus fumigatus)
Status
Unreviewed-Annotation score: Annotation score: 1 out of 5-Experimental evidence at protein leveli

Functioni

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei37 – 371FADCombined sources
Binding sitei54 – 541FAD; via amide nitrogen and carbonyl oxygenCombined sources
Binding sitei187 – 1871FAD; via amide nitrogen and carbonyl oxygenCombined sources

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi16 – 172FADCombined sources
Nucleotide bindingi43 – 475FADCombined sources
Nucleotide bindingi335 – 3373FADCombined sources
Nucleotide bindingi366 – 3683FADCombined sources

GO - Molecular functioni

Complete GO annotation...

Keywords - Ligandi

FADCombined sources, Flavoprotein, Nucleotide-bindingCombined sources

Names & Taxonomyi

Protein namesi
Submitted name:
Fructosyl amine: oxygen oxidoreductaseImported
OrganismiNeosartorya fumigata (Aspergillus fumigatus)Imported
Taxonomic identifieri746128 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3DJDX-ray1.75A/B1-438[»]
3DJEX-ray1.60A/B1-438[»]
ProteinModelPortaliP78573.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP78573.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini9 – 379371DAOInterPro annotationAdd
BLAST

Family and domain databases

Gene3Di3.50.50.60. 3 hits.
InterProiIPR006076. FAD-dep_OxRdtase.
IPR023753. FAD/NAD-binding_dom.
[Graphical view]
PfamiPF01266. DAO. 1 hit.
[Graphical view]
SUPFAMiSSF51905. SSF51905. 2 hits.

Sequencei

Sequence statusi: Complete.

P78573-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAVTKSSSLL IVGAGTWGTS TALHLARRGY TNVTVLDPYP VPSAISAGND
60 70 80 90 100
VNKVISSGQY SNNKDEIEVN EILAEEAFNG WKNDPLFKPY YHDTGLLMSA
110 120 130 140 150
CSQEGLDRLG VRVRPGEDPN LVELTRPEQF RKLAPEGVLQ GDFPGWKGYF
160 170 180 190 200
ARSGAGWAHA RNALVAAARE AQRMGVKFVT GTPQGRVVTL IFENNDVKGA
210 220 230 240 250
VTGDGKIWRA ERTFLCAGAS AGQFLDFKNQ LRPTAWTLVH IALKPEERAL
260 270 280 290 300
YKNIPVIFNI ERGFFFEPDE ERGEIKICDE HPGYTNMVQS ADGTMMSIPF
310 320 330 340 350
EKTQIPKEAE TRVRALLKET MPQLADRPFS FARICWCADT ANREFLIDRH
360 370 380 390 400
PQYHSLVLGC GASGRGFKYL PSIGNLIVDA MEGKVPQKIH ELIKWNPDIA
410 420 430
ANRNWRDTLG RFGGPNRVMD FHDVKEWTNV QYRDISKL
Length:438
Mass (Da):48,932
Last modified:May 1, 1997 - v1
Checksum:iFBC8A3E5D89D02AE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U82830 mRNA. Translation: AAC49711.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U82830 mRNA. Translation: AAC49711.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3DJDX-ray1.75A/B1-438[»]
3DJEX-ray1.60A/B1-438[»]
ProteinModelPortaliP78573.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP78573.

Family and domain databases

Gene3Di3.50.50.60. 3 hits.
InterProiIPR006076. FAD-dep_OxRdtase.
IPR023753. FAD/NAD-binding_dom.
[Graphical view]
PfamiPF01266. DAO. 1 hit.
[Graphical view]
SUPFAMiSSF51905. SSF51905. 2 hits.
ProtoNetiSearch...

Publicationsi

  1. "Molecular cloning and expression of amadoriase isoenzyme (fructosyl amine:oxygen oxidoreductase, EC 1.5.3) from Aspergillus fumigatus."
    Takahashi M., Pischetsrieder M., Monnier V.M.
    J. Biol. Chem. 272:12505-12507(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
  2. "Crystal structure of the deglycating enzyme fructosamine oxidase (FAOX-II)."
    Collard F., Zhang J., Nemet I., Qanungo K.R., Monnier V.M., Yee V.C.
    Submitted (JUN-2008) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) IN COMPLEX WITH FAD, X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) IN COMPLEX WITH FAD.

Entry informationi

Entry nameiP78573_ASPFM
AccessioniPrimary (citable) accession number: P78573
Entry historyi
Integrated into UniProtKB/TrEMBL: May 1, 1997
Last sequence update: May 1, 1997
Last modified: March 16, 2016
This is version 67 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources

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.