UniProtKB - Q2I8V6 (AFR_ENSAD)

>sp|Q2I8V6|AFR_ENSAD 1,5-anhydro-D-fructose reductase OS=Ensifer adhaerens OX=106592 GN=afr PE=1 SV=1
MNRWGLIGASTIAREWVIGAIRATGGEVVSMMSTSAERGAAYATENGIGKSVTSVEELVG
DPDVDAVYVSTTNELHREQTLAAIRAGKHVLCEKPLAMTLEDAREMVVAAREAGVVLGTN
HHLRNAAAHRAMRDAIAEGRIGRPIAARVFHAVYLPPHLQGWRLERPEAGGGVILDITVH
DADTLRFVLNDDPAEAVAISHSAGMGKEGVEDGVMGGVRFQSGVIAQFHDAFTTKFAETG
FEVHGTEGSLIGRNVMTQKPVGTVTLRNAEGESQLPLDPANLYETALAAFHSAIEGHGQP
SATGEDGVWSLATGLAVVKAAATGQAAEIETGL

Entry version 51 (02 Dec 2020)
Sequence version 1 (07 Mar 2006)
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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
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Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
+
NADP⁺
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Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
=
1,5-anhydro-D-fructose
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Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
+
H⁺
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Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
+
NADPH
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Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
1 Publication
Manual assertion based on experiment inⁱ
- Ref.1
  "Catabolism of 1,5-anhydro-D-fructose in Sinorhizobium morelense S-30.7.5: discovery, characterization, and overexpression of a new 1,5-anhydro-D-fructose reductase and its application in sugar analysis and rare sugar synthesis."
  Kuehn A., Yu S., Giffhorn F.
  Appl. Environ. Microbiol. 72:1248-1257(2006) [PubMed] [Europe PMC] [Abstract]
  Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-25, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, MASS SPECTROMETRY, SUBUNIT.
EC:
1.1.1.292
- Search proteins in UniProtKB for this EC number.
- See the description of this EC number in ENZYME.
1 Publication
Manual assertion based on experiment inⁱ
- Ref.1
  "Catabolism of 1,5-anhydro-D-fructose in Sinorhizobium morelense S-30.7.5: discovery, characterization, and overexpression of a new 1,5-anhydro-D-fructose reductase and its application in sugar analysis and rare sugar synthesis."
  Kuehn A., Yu S., Giffhorn F.
  Appl. Environ. Microbiol. 72:1248-1257(2006) [PubMed] [Europe PMC] [Abstract]
  Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-25, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, MASS SPECTROMETRY, SUBUNIT.
Source:
Rhea
Search for this reaction in UniProtKB.
See the description of this reaction in Rhea.
. Show »« Hide
1,5-anhydro-D-mannitol
zoom
+
NADP⁺
zoom
=
1,5-anhydro-D-fructose
zoom
+
H⁺
+
NADPH

Kineticsⁱ

V_max=
500 µmol/min/mg enzyme
1 Publication
Manual assertion based on experiment inⁱ
- Ref.1
  "Catabolism of 1,5-anhydro-D-fructose in Sinorhizobium morelense S-30.7.5: discovery, characterization, and overexpression of a new 1,5-anhydro-D-fructose reductase and its application in sugar analysis and rare sugar synthesis."
  Kuehn A., Yu S., Giffhorn F.
  Appl. Environ. Microbiol. 72:1248-1257(2006) [PubMed] [Europe PMC] [Abstract]
  Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-25, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, MASS SPECTROMETRY, SUBUNIT.

pH dependenceⁱ

Optimum pH is 6.5 at 30 degrees Celsius.1 Publication

Sites

Feature key	Position(s)	DescriptionActions	Length
Binding siteⁱ	38	NADP1 Publication	1
Binding siteⁱ	120	NADP1 Publication	1
Binding siteⁱ	283	NADP1 Publication	1

Regions

Feature key	Position(s)	DescriptionActions	Length
Nucleotide bindingⁱ	9 – 12	NADP1 Publication	4
Nucleotide bindingⁱ	33 – 34	NADP1 Publication	2
Nucleotide bindingⁱ	71 – 76	NADP1 Publication	6
Nucleotide bindingⁱ	93 – 94	NADP1 Publication	2
Nucleotide bindingⁱ	162 – 163	NADP1 Publication	2

GO - Molecular functionⁱ

1,5-anhydro-D-fructose reductase (1,5-anhydro-D-mannitol-forming) activity Source: UniProtKB-EC

Complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Oxidoreductase
Ligand	NADP

Enzyme and pathway databases

BioCycⁱ	MetaCyc:MONOMER-16296
BRENDAⁱ	1.1.1.292, 8538
SABIO-RKⁱ	Q2I8V6

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
Organismⁱ	Ensifer adhaerens (Sinorhizobium morelense)
Taxonomic identifierⁱ	106592 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Rhizobiaceae › Sinorhizobium/Ensifer group › Ensifer

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	10	S → G: Almost no effect. 1 Publication	1
Mutagenesisⁱ	13	A → G: Can use NAD as cosubstrate as well as NADP. 1 Publication	1
Mutagenesisⁱ	33	S → D: No activity. 1 Publication	1
Mutagenesisⁱ	94	K → G: Less than 1% remaining activity. 1 Publication	1
Mutagenesisⁱ	176	D → A: Less than 1% remaining activity. 1 Publication	1
Mutagenesisⁱ	180	H → A: Less than 2% remaining activity. 1 Publication	1
Mutagenesisⁱ	206	G → I: No effect. 1 Publication	1

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000382696	1 – 333	1,5-anhydro-D-fructose reductaseAdd BLAST		333

Interactionⁱ

Subunit structureⁱ

Monomer.

2 Publications

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Beta strandⁱ	3 – 8	Combined sources	6
Helixⁱ	11 – 15	Combined sources	5
Helixⁱ	17 – 23	Combined sources	7
Beta strandⁱ	27 – 32	Combined sources	6
Helixⁱ	36 – 45	Combined sources	10
Helixⁱ	55 – 59	Combined sources	5
Beta strandⁱ	66 – 69	Combined sources	4
Helixⁱ	73 – 75	Combined sources	3
Helixⁱ	76 – 85	Combined sources	10
Beta strandⁱ	89 – 92	Combined sources	4
Beta strandⁱ	94 – 96	Combined sources	3
Helixⁱ	100 – 113	Combined sources	14
Beta strandⁱ	117 – 119	Combined sources	3
Helixⁱ	123 – 125	Combined sources	3
Helixⁱ	127 – 137	Combined sources	11
Turnⁱ	138 – 141	Combined sources	4
Beta strandⁱ	142 – 152	Combined sources	11
Helixⁱ	157 – 159	Combined sources	3
Helixⁱ	162 – 164	Combined sources	3
Turnⁱ	167 – 170	Combined sources	4
Helixⁱ	173 – 176	Combined sources	4
Helixⁱ	178 – 189	Combined sources	12
Beta strandⁱ	193 – 201	Combined sources	9
Beta strandⁱ	204 – 206	Combined sources	3
Beta strandⁱ	212 – 220	Combined sources	9
Beta strandⁱ	225 – 233	Combined sources	9
Beta strandⁱ	240 – 247	Combined sources	8
Beta strandⁱ	249 – 254	Combined sources	6
Beta strandⁱ	256 – 260	Combined sources	5
Beta strandⁱ	263 – 268	Combined sources	6
Beta strandⁱ	271 – 274	Combined sources	4
Helixⁱ	282 – 294	Combined sources	13
Beta strandⁱ	301 – 303	Combined sources	3
Helixⁱ	304 – 323	Combined sources	20

Show more details

3D structure databases

SMRⁱ	Q2I8V6
ModBaseⁱ	Search...
PDBe-KBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ	Q2I8V6

EvolutionaryTraceⁱ

Q2I8V6

Family & Domainsⁱ

Sequence similaritiesⁱ

Belongs to the Gfo/Idh/MocA family.Curated

Family and domain databases

InterProⁱ	View protein in InterPro IPR004104, Gfo/Idh/MocA-like_OxRdtase_C IPR036291, NAD(P)-bd_dom_sf IPR000683, Oxidoreductase_N
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF01408, GFO_IDH_MocA, 1 hit PF02894, GFO_IDH_MocA_C, 1 hit
SUPFAMⁱ	SSF51735, SSF51735, 1 hit

Sequenceⁱ

Sequence statusⁱ: Complete.

Q2I8V6-1 [UniParc]FASTA Add to basket

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        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

Mass spectrometryⁱ

Molecular mass is 35100±130 Da. Determined by MALDI. 1 Publication

Sequence databases

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

Select the link destinations:
EMBLⁱ
GenBankⁱ
DDBJⁱ

Links Updated

DQ140417 Genomic DNA Translation: ABA25865.1

Genome annotation databases

KEGGⁱ	ag:ABA25865

KEGGⁱ

ag:ABA25865

Protein	Similar proteins		Species	Score	Length	Source
Q2I8V6	Oxidoreductase domain protein		Ensifer adhaerens OV14		333	UniRef90_Q2I8V6
Gfo/Idh/MocA family oxidoreductase		Ensifer sp. NM-2		333
Fructose reductase		Sinorhizobium sp. A49		333
1,5-anhydro-D-fructose reductase		Ensifer sp. M14		333
+6

Protein	Similar proteins		Species	Score	Length	Source
Q2I8V6	1,5-anhydro-D-fructose reductase	)	RHIME		333	UniRef50_Q2I8V6
Fructose reductase		Sinorhizobium sp. A49		333
1,5-anhydro-D-fructose reductase		Ensifer sp. M14		333
Oxidoreductase domain protein		Ensifer adhaerens OV14		333
Gfo/Idh/MocA family oxidoreductase		Ensifer sp. NM-2		333
+669

Cross-referencesⁱ

Sequence databases

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

Select the link destinations:
EMBLⁱ
GenBankⁱ
DDBJⁱ

Links Updated

DQ140417 Genomic DNA Translation: ABA25865.1

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	2GLX	X-ray	2.20	A/B/C/D/E/F	2-333	[»]
SMRⁱ	Q2I8V6
ModBaseⁱ	Search...
PDBe-KBⁱ	Search...

Genome annotation databases

KEGGⁱ	ag:ABA25865

KEGGⁱ

ag:ABA25865

Enzyme and pathway databases

BioCycⁱ	MetaCyc:MONOMER-16296
BRENDAⁱ	1.1.1.292, 8538
SABIO-RKⁱ	Q2I8V6

Miscellaneous databases

EvolutionaryTraceⁱ	Q2I8V6

EvolutionaryTraceⁱ

Q2I8V6

Family and domain databases

InterProⁱ	View protein in InterPro IPR004104, Gfo/Idh/MocA-like_OxRdtase_C IPR036291, NAD(P)-bd_dom_sf IPR000683, Oxidoreductase_N
Pfamⁱ	View protein in Pfam PF01408, GFO_IDH_MocA, 1 hit PF02894, GFO_IDH_MocA_C, 1 hit
SUPFAMⁱ	SSF51735, SSF51735, 1 hit
ProtoNetⁱ	Search...
MobiDBⁱ	Search...

Entry informationⁱ

Entry nameⁱ	AFR_ENSAD
Accessionⁱ	Q2I8V6Primary (citable) accession number: Q2I8V6
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	September 1, 2009
	Last sequence update:	March 7, 2006
	Last modified:	December 2, 2020
	This is version 51 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Prokaryotic Protein Annotation Program

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UniProtKB - Q2I8V6 (AFR_ENSAD)

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1,5-anhydro-D-fructose reductase

afr

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<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

pH dependencei

Sites

Regions

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Family and domain databases

<p>This subsection of the 'Sequence' section reports information derived from mass spectrometry experiments done on the entire protein or on biologically active derived peptide(s).<p><a href='/help/mass_spectrometry' target='_top'>More...</a></p>Mass spectrometryi

Sequence databases

Genome annotation databases

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Genome annotation databases

Enzyme and pathway databases

Miscellaneous databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

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Functionⁱ

Catalytic activityⁱ

Kineticsⁱ

pH dependenceⁱ

GO - Molecular functionⁱ

Names & Taxonomyⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Mass spectrometryⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ