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Protein

1,5-anhydro-D-fructose reductase

Gene

afr

Organism
Ensifer adhaerens (Sinorhizobium morelense)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Catalyzes the NADPH-specific reduction of 1,5-anhydro-D-fructose to 1,5-anhydro-D-mannitol. Also shows some activity against structurally related compounds such as 3-keto-1,5-anhydro-D-fructose, D-glucosone and D-xylosone. The enzyme cannot use NADH as cosubstrate.

Catalytic activityi

1,5-anhydro-D-mannitol + NADP+ = 1,5-anhydro-D-fructose + NADPH.1 Publication

Kineticsi

  1. KM=8.4 mM for 1,5-anhydro-D-fructose1 Publication
  2. KM=11 mM for D-glucosone1 Publication
  3. KM=0.2 mM for NADPH1 Publication
  1. Vmax=500 µmol/min/mg enzyme1 Publication

pH dependencei

Optimum pH is 6.5 at 30 degrees Celsius.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei38NADP1 Publication1
Binding sitei120NADP1 Publication1
Binding sitei283NADP1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi9 – 12NADP1 Publication4
Nucleotide bindingi33 – 34NADP1 Publication2
Nucleotide bindingi71 – 76NADP1 Publication6
Nucleotide bindingi93 – 94NADP1 Publication2
Nucleotide bindingi162 – 163NADP1 Publication2

GO - Molecular functioni

Keywordsi

Molecular functionOxidoreductase
LigandNADP

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-16296
BRENDAi1.1.1.292 8538
SABIO-RKiQ2I8V6

Names & Taxonomyi

Protein namesi
Recommended name:
1,5-anhydro-D-fructose reductase (EC:1.1.1.292)
Short name:
Anhydrofructose reductase
Alternative name(s):
1,5-anhydro-D-fructose reductase (1,5-anhydro-D-mannitol-forming)
Gene namesi
Name:afr
OrganismiEnsifer adhaerens (Sinorhizobium morelense)
Taxonomic identifieri106592 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesRhizobiaceaeSinorhizobium/Ensifer groupEnsifer

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi10S → G: Almost no effect. 1 Publication1
Mutagenesisi13A → G: Can use NAD as cosubstrate as well as NADP. 1 Publication1
Mutagenesisi33S → D: No activity. 1 Publication1
Mutagenesisi94K → G: Less than 1% remaining activity. 1 Publication1
Mutagenesisi176D → A: Less than 1% remaining activity. 1 Publication1
Mutagenesisi180H → A: Less than 2% remaining activity. 1 Publication1
Mutagenesisi206G → I: No effect. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003826961 – 3331,5-anhydro-D-fructose reductaseAdd BLAST333

Interactioni

Subunit structurei

Monomer.2 Publications

Structurei

Secondary structure

1333
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliQ2I8V6
SMRiQ2I8V6
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ2I8V6

Family & Domainsi

Sequence similaritiesi

Belongs to the Gfo/Idh/MocA family.Curated

Phylogenomic databases

KOiK19181

Family and domain databases

InterProiView protein in InterPro
IPR036291 NAD(P)-bd_dom_sf
IPR000683 Oxidoreductase_N
IPR004104 OxRdtase_C
PfamiView protein in Pfam
PF01408 GFO_IDH_MocA, 1 hit
PF02894 GFO_IDH_MocA_C, 1 hit
SUPFAMiSSF51735 SSF51735, 1 hit

Sequencei

Sequence statusi: Complete.

Q2I8V6-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MNRWGLIGAS TIAREWVIGA IRATGGEVVS MMSTSAERGA AYATENGIGK
60 70 80 90 100
SVTSVEELVG DPDVDAVYVS TTNELHREQT LAAIRAGKHV LCEKPLAMTL
110 120 130 140 150
EDAREMVVAA REAGVVLGTN HHLRNAAAHR AMRDAIAEGR IGRPIAARVF
160 170 180 190 200
HAVYLPPHLQ GWRLERPEAG GGVILDITVH DADTLRFVLN DDPAEAVAIS
210 220 230 240 250
HSAGMGKEGV EDGVMGGVRF QSGVIAQFHD AFTTKFAETG FEVHGTEGSL
260 270 280 290 300
IGRNVMTQKP VGTVTLRNAE GESQLPLDPA NLYETALAAF HSAIEGHGQP
310 320 330
SATGEDGVWS LATGLAVVKA AATGQAAEIE TGL
Length:333
Mass (Da):35,010
Last modified:March 7, 2006 - v1
Checksum:iA6A088EC1075C917
GO

Mass spectrometryi

Molecular mass is 35100±130 Da from positions 1 - 333. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ140417 Genomic DNA Translation: ABA25865.1

Genome annotation databases

KEGGiag:ABA25865

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ140417 Genomic DNA Translation: ABA25865.1

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2GLXX-ray2.20A/B/C/D/E/F2-333[»]
ProteinModelPortaliQ2I8V6
SMRiQ2I8V6
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGiag:ABA25865

Phylogenomic databases

KOiK19181

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-16296
BRENDAi1.1.1.292 8538
SABIO-RKiQ2I8V6

Miscellaneous databases

EvolutionaryTraceiQ2I8V6

Family and domain databases

InterProiView protein in InterPro
IPR036291 NAD(P)-bd_dom_sf
IPR000683 Oxidoreductase_N
IPR004104 OxRdtase_C
PfamiView protein in Pfam
PF01408 GFO_IDH_MocA, 1 hit
PF02894 GFO_IDH_MocA_C, 1 hit
SUPFAMiSSF51735 SSF51735, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiAFR_ENSAD
AccessioniPrimary (citable) accession number: Q2I8V6
Entry historyiIntegrated into UniProtKB/Swiss-Prot: September 1, 2009
Last sequence update: March 7, 2006
Last modified: October 25, 2017
This is version 46 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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Main funding by: National Institutes of Health

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